ACL_RS02000

Uniprot: A9NF91
Description: 2,3-bisphosphoglycerate-independent 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:0000255|HAMAP-Rule:MF_01038}.
Cofactor: COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01038}; ; Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01038}
Enzyme regulation:
Function [CC]: FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
Pathway: PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_01038}.
Active site: ACT_SITE 62 62 Phosphoserine intermediate. {ECO:0000255|HAMAP-Rule:MF_01038}.
Binding site: BINDING 123 123 Substrate. {ECO:0000255|HAMAP-Rule:MF_01038}.; BINDING 181 181 Substrate. {ECO:0000255|HAMAP-Rule:MF_01038}.; BINDING 187 187 Substrate. {ECO:0000255|HAMAP-Rule:MF_01038}.; BINDING 335 335 Substrate. {ECO:0000255|HAMAP-Rule:MF_01038}.
Calcium binding:
DNA binding:
Metal binding: METAL 12 12 Manganese 2. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 62 62 Manganese 2. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 402 402 Manganese 1. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 406 406 Manganese 1. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 444 444 Manganese 2. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 445 445 Manganese 2. {ECO:0000255|HAMAP-Rule:MF_01038}.; METAL 462 462 Manganese 1. {ECO:0000255|HAMAP-Rule:MF_01038}.
Nucleotide binding:
Site:
Gene names (primary): gpmI
Gene names (synonym):
Mass: 55,835
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000255|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: CHAIN 1 511 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. /FTId=PRO_1000084295.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. {ECO:0000255|HAMAP-Rule:MF_01038}.
Protein families: BPG-independent phosphoglycerate mutase family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 154 155 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_01038}.; REGION 252 255 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_01038}.
EMBL: CP000896
ProteinModelPortal: A9NF91
MEROPS:
EnsemblBacteria KO: ABX81021
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

419547-421083(-)

>nucleotide sequence
TTATATTTTTTCGATTAATGATGTACCAGTCATTGCTTTAGGTTTTTCAATACCTAGTAA
ATCTAATAATGTAGGTGCAACGTCACATAGTGCACCACTATTTAATTTAATACCTTTTTT
AGTTACTACAACAGGTACTAAGTTTGTTGTATGTGCTGTATGTGGTTTACCTTCTTGATC
ACGCATTTGTTCTGCATTACCATGGTCAGCTAAGATGATTGCTACACCACCAAGTTCATT
GATGATGAAGTCTGTAACTTTACCAACACACTCAACAGTTACTTCAACTGCCTTTTTAGT
AGCTTCAATATTTCCTGTATGTCCTACCATATCAGGGTTTGCGAAGTTAAGAATCATTGT
TTGATATTCACCTGTTTTTAATGCTGCAATGACTTTATCAGTTAGTTCATATGCTGACAT
TTCAGGCTTTAGATCATAGGTTGGAACCTTTGGTGATTCGGCTAGAATTCTAGTTGAGTT
TGCTAAAGGTACTTCTTTACCACCGTCAAAGAAGAAGGTAACGTGGGGGTATTTTTCAGT
CTCAGCTGCACGGATTTGTTTGAAACCATTTTTTTCAATAACTTCACCGTATAGATCATC
AAAAGTTTGAAGTTCGAATGCTAAAGGACCTTTAACAGTTTCTTTATAATGCATCATAGA
TACTAAGAAGATATTCTTTGGTGCTTTAGAAACATTTAACATTGGTTTACCTTCTGTGTA
AATTGTTTTAGCAGCACTTGGATTAGATAATGCAGTGGCAATACGAATTGCTCTGTCAGG
TCTAAAGTTTGCAAAGATGACAGCATCATCGTTTTCGATTAAACCTTTGTCGTTTACGAT
AAATGGTTTAATGAATTCATCTTGAATACCACTCTTATAACTTGATTCAATACCGTCTAG
TGCACTATTAAAGTGTGGGCCATCGCCTAATGTCATTGCATCAAATGCTAATTGAACACG
GTCCCAGTTGTTGTCTCTATCCATTGCATAGAATCTACCTGAAACTGTTGCTACATTAAA
ACCATAATCTACTAAAGTTTTAACGAAACCATAACCAGATTCTTGTGGCGTATCACGGCC
ATCAGTGAATACATGTAGGTAAGTTCTGTCTAAGATGTTTTGTTGTTTAGCAAAATCGTA
TAATGCTAAATAGTGTCCCATTTGGGCATGTACACCACCATCAGAAACTAGACCCATAAT
GTGTAGTTTAGAATTATGTTTCTTAGCATGTGCTACTGCATCTAAAAATGCTTGATTCTT
AAAAAAGGAACCATCTTTAATAGCAACATTAATTCTAGAAAGTGATTGCCAAACAATACG
TCCAGCACCTAGGTTTAAGTGACCTACTTCACTATTACCCATTTGACCTTCTGGTAATCC
AACTGCCTCACCAGATGTTACTAGTGTGCTATTTGGATATTCTTTAAGTAAGTTGTCTAA
ATATGTTGTATCTGCAAGTGTTACAGAGTTTGAATCAGATGCTGGAGCTATACCAAGACC
ATCCATGATAATTAAAGCTGCAAATTTTTCTTTCAT

>protein sequence
MKEKFAALIIMDGLGIAPASDSNSVTLADTTYLDNLLKEYPNSTLVTSGEAVGLPEGQMG
NSEVGHLNLGAGRIVWQSLSRINVAIKDGSFFKNQAFLDAVAHAKKHNSKLHIMGLVSDG
GVHAQMGHYLALYDFAKQQNILDRTYLHVFTDGRDTPQESGYGFVKTLVDYGFNVATVSG
RFYAMDRDNNWDRVQLAFDAMTLGDGPHFNSALDGIESSYKSGIQDEFIKPFIVNDKGLI
ENDDAVIFANFRPDRAIRIATALSNPSAAKTIYTEGKPMLNVSKAPKNIFLVSMMHYKET
VKGPLAFELQTFDDLYGEVIEKNGFKQIRAAETEKYPHVTFFFDGGKEVPLANSTRILAE
SPKVPTYDLKPEMSAYELTDKVIAALKTGEYQTMILNFANPDMVGHTGNIEATKKAVEVT
VECVGKVTDFIINELGGVAIILADHGNAEQMRDQEGKPHTAHTTNLVPVVVTKKGIKLNS
GALCDVAPTLLDLLGIEKPKAMTGTSLIEKI