(data stored in SCRATCH zone)

SWISSPROT: A4AVV4_MARSH

ID   A4AVV4_MARSH            Unreviewed;       249 AA.
AC   A4AVV4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728730};
DE            Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728682};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=FB2170_01632 {ECO:0000313|EMBL:EAR00034.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00034.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00034.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC         ECO:0000256|SAAS:SAAS01116239};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728615}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728661}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728708}.
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DR   EMBL; CP002157; EAR00034.1; -; Genomic_DNA.
DR   RefSeq; WP_013305020.1; NC_014472.1.
DR   STRING; 313603.FB2170_01632; -.
DR   EnsemblBacteria; EAR00034; EAR00034; FB2170_01632.
DR   KEGG; fbc:FB2170_01632; -.
DR   eggNOG; ENOG4105CP7; Bacteria.
DR   eggNOG; COG0149; LUCA.
DR   HOGENOM; HOG000226413; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   OrthoDB; 1266295at2; -.
DR   BioCyc; MSP313603:G1GNS-588-MONOMER; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVV4.
DR   SWISS-2DPAGE; A4AVV4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728593};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728672};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498630,
KW   ECO:0000313|EMBL:EAR00034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   REGION        9     11       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      233    234       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE     94     94       Electrophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   BINDING     172    172       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   BINDING     212    212       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
SQ   SEQUENCE   249 AA;  26903 MW;  4B56A158FF02C953 CRC64;
     MRSKIVAGNW KMNKNLAETE ALVIELEAKL PNTDAEVMVS PTFVNLASAV SKLQGSKIKV
     IAQNMHNAES GAYTGEISAD MLLNIGIDTV ILGHSERRAY FGETDEILAT KVKAALAKNM
     QIMFCFGEEL NDRKSDNHFK VVESQLRNAL FDLDPSAWSS IILAYEPVWA IGTGETASPE
     QAQEMHAFIR KTIANAFNNE IAENVSILYG GSVKPGNAKE IFSKPDVDGG LIGGAALVAD
     DFVAIINGI
//

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