ID C3T937_ECOLX Unreviewed; 391 AA. AC C3T937; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 11-DEC-2019, entry version 51. DE RecName: Full=Mannose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000611}; DE EC=5.3.1.8 {ECO:0000256|RuleBase:RU000611}; GN ORFNames=ECs2319 {ECO:0000313|EMBL:ACI83221.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI83221.1}; RN [1] {ECO:0000313|EMBL:ACI83221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=493/89 {ECO:0000313|EMBL:ACI83221.1}; RX PubMed=19439656; DOI=10.1073/pnas.0812949106; RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., RA Sawyer S.A., Whittam T.S., Tarr P.I.; RT "A precise reconstruction of the emergence and constrained radiations of RT Escherichia coli O157 portrayed by backbone concatenomic analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate; CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527; CC EC=5.3.1.8; Evidence={ECO:0000256|RuleBase:RU000611}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR001480-2, CC ECO:0000256|RuleBase:RU000611}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001480-2, CC ECO:0000256|RuleBase:RU000611}; CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family. CC {ECO:0000256|RuleBase:RU004189}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU900670; ACI83221.1; -; Genomic_DNA. DR RefSeq; WP_001170636.1; NZ_NJVH01000006.1. DR PATRIC; fig|562.7216.peg.5605; -. DR eggNOG; ENOG4105EIP; Bacteria. DR eggNOG; COG1482; LUCA. DR HOGENOM; HOG000241278; -. DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 2. DR InterPro; IPR001250; Man6P_Isoase-1. DR InterPro; IPR016305; Mannose-6-P_Isomerase. DR InterPro; IPR018050; Pmannose_isomerase-type1_CS. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR10309; PTHR10309; 1. DR Pfam; PF01238; PMI_typeI; 1. DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1. DR PRINTS; PR00714; MAN6PISMRASE. DR SUPFAM; SSF51182; SSF51182; 1. DR TIGRFAMs; TIGR00218; manA; 1. DR PROSITE; PS00965; PMI_I_1; 1. DR PROSITE; PS00966; PMI_I_2; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|RuleBase:RU000611, ECO:0000313|EMBL:ACI83221.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001480-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR001480-2, ECO:0000256|RuleBase:RU000611}. FT ACT_SITE 274 FT /evidence="ECO:0000256|PIRSR:PIRSR001480-1" FT METAL 97 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT METAL 99 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT METAL 134 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT METAL 255 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" SQ SEQUENCE 391 AA; 42832 MW; 7E18DECF3C0DF873 CRC64; MQKLINSVQN YAWGSKTALT ELYGMENPSS QPMAELWIGA HPKSSSRVQN AAGDIVSLRD VIESDKSTLL GEAVAKRFGE LPFLFKVLCA AQPLSIQVHP NKHKSEIGFA KENAAGIPMD AAERNYKDPN HKPELVFALT PFLAMNAFRE FSEIVSLLQP VAGAHPAIAH FLQQPDAERL SELFASLLNM QGEEKSRALA ILKSALDSQQ GEPWQTIRLI SEFYPDDSGL FSPLLLNVVK LNPGEAMFLF AETPHAYLQG VALEVMANSD NVLRAGLTPK YIDIPELVAN VKFEAKPANQ LLTQPVKQGA ELDFPIPVDD FAFSLHDLSD KETTISQQSA AILFCVEGDA TLWKGSQQLQ LKPGESAFIA ANESPVTVKG HGRLARVYNK L //