SPM_005360

Uniprot: A0A037UR17
Description: phosphoglyceromutase
EC number: 5.4.2.12
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00058354}.
Cofactor: COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-Rule:MF_01038}; ; Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01038}
Enzyme regulation:
Function [CC]: FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00368562}.
Pathway: PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00058352}.
Active site: ACT_SITE 63 63 Phosphoserine intermediate. {ECO:0000256|HAMAP-Rule:MF_01038}.
Binding site: BINDING 124 124 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 192 192 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 338 338 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.
Calcium binding:
DNA binding:
Metal binding: METAL 13 13 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 63 63 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 416 416 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 420 420 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 457 457 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 458 458 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 475 475 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.
Nucleotide binding:
Site:
Gene names (primary): gpmI
Gene names (synonym):
Mass: 58,096
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
Gene ontology (GO): cytoplasm [GO:0005737]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity [GO:0046537]; manganese ion binding [GO:0030145]; glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096]
Gene ontology IDs: GO:0005737; GO:0006007; GO:0006096; GO:0030145; GO:0046537
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00559283}.
Protein families: BPG-independent phosphoglycerate mutase family
Coiled coil:
Domain [FT]: DOMAIN 6 510 Metalloenzyme. {ECO:0000259|Pfam:PF01676}.; DOMAIN 83 300 iPGM_N. {ECO:0000259|Pfam:PF06415}.
Motif:
Region: REGION 154 155 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01038}.; REGION 259 262 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01038}.
EMBL: AGBZ02000004
ProteinModelPortal: A0A037UR17
MEROPS:
EnsemblBacteria KO: KAI92165
UniPathway:
CDD:
Gene3D:
HAMAP: 3.40.1450.10;3.40.720.10
InterPro: MF_01038
PANTHER: IPR017849;IPR017850;IPR011258;IPR006124;IPR005995
PIRSF:
PRINTS: PIRSF001492
PROSITE:
Pfam:
ProDom: PF06415;PF01676
SMART:
SUPFAM:
TIGRFAMs: SSF53649;SSF64158

135594-137172(+)

>nucleotide sequence
ATGAAAGTTAAACAACCAATTTTATTGGCAATTCTTGATGGATGAGGAATTGCTCCTGAT
TCAAAAGGAAATGCTGTAACACAAGGACATATGGTGAATGTTGAAAAATTAAAAACAAAA
TATCCATGAGTCTCAGCACATGCGGCAGGAGAATGAGTTGGTTTACCAGAAGGACAAATG
GGAAATTCTGAAGTTGGACATATTCATTTAGGAGCAGGTCGCATTAAATATGAATCATTA
ACTTTAATTAATAAAGCAATTAAAGATGGAACATTTAATCAAAATCCAGAACTTTTAGCG
GCAATTAATTTTGCAAAAAAAAGTAATGGTGCCTTTCATATTATGGGGTTATTTTCTGAT
GGTGGTGTTCACTCGCATTTAAACCATATTTTTGCTGCTTATAAATTAGCAGCACAAGAA
GGAATAAAAGAGATTTACTTGCATATTTTTGGCGATGGACGTGATACGAAACCAGAATGT
ATTAAAATTTACCTTGAACAATTTCAACAATTACAAAACCAATTAAAAGTTGGGGAAATT
GCAACAATTGGTGGTCGTTATTACGCAATGGATCGTGATAAAAAATATGACCGAGTGCAA
ATTGCTTATGATGTTTTAGTTTCAAGAAAGGGTTCAGAATTTAGTGACCCAATAGAGTAT
ATTAACCGTGAATATCAAGCTGGTCGCAATGATGAATTTTTAATGCCAGCATATAATATT
AATACCCCAAAAGGTTATATTAAATCAGGTGATGGTGTCTTTTTTGCTAATTTTCGCCCG
GACCGTGCTATTGCAATAGCTTCAGCTTTAACAAATCCTAATTTTCCGGGTAATGAAGCA
CAAACTTATTTTATGCCGAAATTACATGATATTTATTTTGTTTCAATGATGGAATATGCA
GAAACAGTTGCTTCAAAACATGTTGCTTTTAAACCAATTGAAGTTGTTAATGGTTTAGGA
GAATGATTAAGTAAAAAAGGCTATCGACAACTACGAATTGCTGAAACAGAAAAAATTGCT
CATGTTACATTTTTCTTTGATGGTGGAAAAGATTATTTTAAAAATGGTTTAGCAACACAA
GCCGAAATTACATTAACAGGGGCTTCGGCAGATTTAATTCCATCGCCAAAAGTAGCAACT
TATGATTTAAAGCCAGAAATGTCAGCATATGAAATTACTGATAAGTTAATTACTGAACTT
AATCAAAATGAATTTGATGTTATTATTTTAAATTTTGCAAATTGTGATATGGTTGGTCAT
ACTGGAATCTTGCCAGCGGCAATAGAAGCAGTTAAAACTATTGATAATTGTCTTGGCAAA
ATTTATACAGCAATTCAAAAAGTTAACGGAATTATGATTATTACTGCTGACCACGGAAAT
GCTGAAATTATGATAGATGAAACGGGTGGTCCTAATAAAAAACATACTTCACAATTGGTT
CCAATTATTATTACCAAAGAAGGGTTACAATTACGACAAGATAATCCGGCAATTGCTGAT
ATTGCTCCGACAATTTTAGATTTATTAGGTGAAGAGATTCCTCCTGAAATGACACAACCA
TCATTAATTATTAAGTAA

>protein sequence
MKVKQPILLAILDGWGIAPDSKGNAVTQGHMVNVEKLKTKYPWVSAHAAGEWVGLPEGQM
GNSEVGHIHLGAGRIKYESLTLINKAIKDGTFNQNPELLAAINFAKKSNGAFHIMGLFSD
GGVHSHLNHIFAAYKLAAQEGIKEIYLHIFGDGRDTKPECIKIYLEQFQQLQNQLKVGEI
ATIGGRYYAMDRDKKYDRVQIAYDVLVSRKGSEFSDPIEYINREYQAGRNDEFLMPAYNI
NTPKGYIKSGDGVFFANFRPDRAIAIASALTNPNFPGNEAQTYFMPKLHDIYFVSMMEYA
ETVASKHVAFKPIEVVNGLGEWLSKKGYRQLRIAETEKIAHVTFFFDGGKDYFKNGLATQ
AEITLTGASADLIPSPKVATYDLKPEMSAYEITDKLITELNQNEFDVIILNFANCDMVGH
TGILPAAIEAVKTIDNCLGKIYTAIQKVNGIMIITADHGNAEIMIDETGGPNKKHTSQLV
PIIITKEGLQLRQDNPAIADIAPTILDLLGEEIPPEMTQPSLIIK