GCW_03285

Uniprot: A0A0F6CL67
Description: phosphoglycerate mutase
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 60 60 Phosphoserine intermediate. {ECO:0000256|HAMAP-Rule:MF_01038}.
Binding site: BINDING 121 121 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 181 181 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 187 187 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.; BINDING 330 330 Substrate. {ECO:0000256|HAMAP-Rule:MF_01038}.
Calcium binding:
DNA binding:
Metal binding: METAL 10 10 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 60 60 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 396 396 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 400 400 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 437 437 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 438 438 Manganese 2. {ECO:0000256|HAMAP-Rule:MF_01038}.; METAL 455 455 Manganese 1. {ECO:0000256|HAMAP-Rule:MF_01038}.
Nucleotide binding:
Site:
Gene names (primary): gpmI
Gene names (synonym):
Mass: 56,520
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 2 491 Metalloenzyme. {ECO:0000259|Pfam:PF01676}.; DOMAIN 80 293 iPGM_N. {ECO:0000259|Pfam:PF06415}.
Motif:
Region: REGION 150 151 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01038}.; REGION 256 259 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01038}.
EMBL: CP006916
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: AHB99839
UniPathway: K15633
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
787000-788512(-)

>nucleotide sequence
TTAAATTAGTGGTTCTTGATCCATCTCTTCAGGAATTTGAATCTCTAGATATTTTAGGAT
CGTTGGGGCAACGTTAGCTAAAATCCCTTCTTTTTTAGTAAATTTAACGTTTGGATCGGT
GATACTAAAAGGCACAACGTTTGTTGTGTGTTTGGTTACCTTTTGGTTATTTTCATCGAT
CATCTCTTCGGCATTACCATGATCAGCCGTAAAGAACACCGTAATATTATTCTTCTTAGC
ATCAGCTAATAATCGACCAATCTCGTGGTCTAGTGCTTCAAGTCCTTTTAGGGTTGCTTC
ATAATTACCAGTATGACCAACCATATCAGGGTTAGCAAAATTTAACACAGTTAGATCGTA
TTTTGTATAAACTTTTAGTAACTGATCAACAATCGCTGCAGCCGACATTTCAGGTGCTAG
GTCATAAGTCTTAACATCTTTTCTTGAAGGAACTAAAACTTTATTTTCGTTTTGATACTC
AACTTCAACACCACCATCAAAAAAGAAGGTAACGTGTGCGTATTTTTCAGTTTCAGCAAT
TCTTAATTGCTTCTTATTAGCATTCTTTAACACTTCACCTAAAGTGTTCTTTTCAATCTT
TGGGGGATAACAGATCGCTGAAGGATTAATTCCTTCGTATTGCATCATAATTACGAAGTA
AAGGTTTTTTCTTTTTAGTTGTGGATGATGATCATAATAGTTCGAACCAAAGATATAATG
ACTTAATTGACGTGCTCGATCTGGTCTGAAATTAGCAAAAACAACACTGTCATTGTCTTG
AATAGTGATCTCATCACTCTTGTAATTATTATTGTAAGCAGGAACAATGAATTCGTCTGT
AATATTTTGTTGATACGAATCCTTTACATAAGTTTTCAGATCAGCAAAACTTTTACCTGT
ATTTGATAAAAGGTTATTGTAAGCTAAATCAATTCGATCCCATCTTTGGTCACGATCCAT
CGCATAGAACCGACCAGAGACCGTACCGATCTTAGTTTTAGTTGCTTCTGCTTTTTTAAT
TAGTTGATCTAAATCAGCTAATAATTGGGTTGGTGGTACGTCTCTACCATCACCAAAGAT
ATGTAAGATTGCAGGTACATTATGTTGATTAGCCAACTCCATGATCGCATAGATATGGTT
AATGTGTGAGTGCACGCCACCATTAGAGACCAATCCCAAGATATGTAGTTTACTATTATT
TTTCTTGGCGTGATCAATCGCATTTAGTAATGCTTGGTTAGTAAAAAACTTCTTGTTTTC
GATCTCTTTATTAATTAAAGATAGACCCGTATAAATAATTCGGCCTGCTCCGATATTTAA
GTGACCAACCTCAGAGTTACCAATCTGATTTTTAGGTAAACCCACAGCTTCACCACTAGC
TTGAAGCATAATTGTGGGATTGTTGTTCATTAAGTTATCTAAATGAGGTGTCTTGGCATT
TTTTACGGCATTACCGTGAGTAGTTGAACTGATTCCATAGCCATCAAGAATCATTAATAG
TGCTTTTTTCAT

>protein sequence
MKKALLMILDGYGISSTTHGNAVKNAKTPHLDNLMNNNPTIMLQASGEAVGLPKNQIGNS
EVGHLNIGAGRIIYTGLSLINKEIENKKFFTNQALLNAIDHAKKNNSKLHILGLVSNGGV
HSHINHIYAIMELANQHNVPAILHIFGDGRDVPPTQLLADLDQLIKKAEATKTKIGTVSG
RFYAMDRDQRWDRIDLAYNNLLSNTGKSFADLKTYVKDSYQQNITDEFIVPAYNNNYKSD
EITIQDNDSVVFANFRPDRARQLSHYIFGSNYYDHHPQLKRKNLYFVIMMQYEGINPSAI
CYPPKIEKNTLGEVLKNANKKQLRIAETEKYAHVTFFFDGGVEVEYQNENKVLVPSRKDV
KTYDLAPEMSAAAIVDQLLKVYTKYDLTVLNFANPDMVGHTGNYEATLKGLEALDHEIGR
LLADAKKNNITVFFTADHGNAEEMIDENNQKVTKHTTNVVPFSITDPNVKFTKKEGILAN
VAPTILKYLEIQIPEEMDQEPLI