ID C3T937_ECOLX Unreviewed; 391 AA. AC C3T937; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 24-JAN-2024, entry version 62. DE RecName: Full=mannose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011956}; DE EC=5.3.1.8 {ECO:0000256|ARBA:ARBA00011956}; DE AltName: Full=Phosphohexomutase {ECO:0000256|ARBA:ARBA00029741}; DE AltName: Full=Phosphomannose isomerase {ECO:0000256|ARBA:ARBA00030762}; GN ORFNames=ECs2319 {ECO:0000313|EMBL:ACI83221.1}; OS Escherichia coli. OC Bacteria; Pseudomonadota; 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|ARBA:ARBA00000757}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR001480-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001480-2}; CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family. CC {ECO:0000256|ARBA:ARBA00010772}. 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_SQPD01000002.1. DR AlphaFoldDB; C3T937; -. DR PATRIC; fig|562.7216.peg.5605; -. 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 CDD; cd07011; cupin_PMI_type_I_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR Gene3D; 1.10.441.10; Phosphomannose Isomerase, domain 2; 1. DR InterPro; IPR001250; Man6P_Isoase-1. DR InterPro; IPR016305; Mannose-6-P_Isomerase. DR InterPro; IPR049071; MPI_cupin_dom. DR InterPro; IPR018050; Pmannose_isomerase-type1_CS. DR InterPro; IPR046457; PMI_typeI_cat. DR InterPro; IPR046458; PMI_typeI_hel. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR NCBIfam; TIGR00218; manA; 1. DR PANTHER; PTHR10309; MANNOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR10309:SF0; MANNOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF21621; MPI_cupin_dom; 1. DR Pfam; PF20511; PMI_typeI_cat; 1. DR Pfam; PF20512; PMI_typeI_hel; 1. DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1. DR PRINTS; PR00714; MAN6PISMRASE. DR SUPFAM; SSF51182; RmlC-like cupins; 1. DR PROSITE; PS00965; PMI_I_1; 1. DR PROSITE; PS00966; PMI_I_2; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ACI83221.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR001480-2}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001480-2}. FT DOMAIN 1..150 FT /note="Phosphomannose isomerase type I catalytic" FT /evidence="ECO:0000259|Pfam:PF20511" FT DOMAIN 157..236 FT /note="Phosphomannose isomerase type I helical insertion" FT /evidence="ECO:0000259|Pfam:PF20512" FT DOMAIN 311..389 FT /note="Mannose-6-phosphate isomerase cupin" FT /evidence="ECO:0000259|Pfam:PF21621" FT ACT_SITE 274 FT /evidence="ECO:0000256|PIRSR:PIRSR001480-1" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" 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 //