(data stored in SCRATCH zone)

SWISSPROT: Q3IF10_PSEHT

ID   Q3IF10_PSEHT            Unreviewed;       458 AA.
AC   Q3IF10;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 83.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743,
GN   ECO:0000313|EMBL:CAI85158.1};
GN   OrderedLocusNames=PSHAa0048 {ECO:0000313|EMBL:CAI85158.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85158.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85158.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000256|HAMAP-
CC       Rule:MF_00743}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
CC       malate from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic
CC       A site, and the non-catalytic B site that may play a role in the
CC       transfer of substrate or product between the active site and the
CC       solvent. Alternatively, the B site may bind allosteric effectors.
CC       {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily. {ECO:0000256|HAMAP-Rule:MF_00743}.
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DR   EMBL; CR954246; CAI85158.1; -; Genomic_DNA.
DR   RefSeq; WP_011326776.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF10; -.
DR   STRING; 326442.PSHAa0048; -.
DR   EnsemblBacteria; CAI85158; CAI85158; PSHAa0048.
DR   KEGG; pha:PSHAa0048; -.
DR   PATRIC; fig|326442.8.peg.46; -.
DR   eggNOG; ENOG4105C9Q; Bacteria.
DR   eggNOG; COG0114; LUCA.
DR   HOGENOM; HOG000061736; -.
DR   KO; K01679; -.
DR   OMA; RIATIWN; -.
DR   OrthoDB; POG091H01XG; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP.
DR   CDD; cd01362; Fumarase_classII; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00743; FumaraseC; 1.
DR   InterPro; IPR005677; Fum_hydII.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IF10.
DR   SWISS-2DPAGE; Q3IF10.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00674282,
KW   ECO:0000313|EMBL:CAI85158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN       12    336       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      402    454       FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
FT   REGION       98    100       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      123    126       Substrate binding (B site).
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   REGION      133    135       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      318    320       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   ACT_SITE    182    182       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   ACT_SITE    312    312       {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   BINDING     181    181       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   BINDING     313    313       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   SITE        325    325       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
SQ   SEQUENCE   458 AA;  48738 MW;  4E482E75689200D3 CRC64;
     MTQFRTESDS MGELQVPANA LYQAQTQRAV NNFAISGLAM PKQFITALAY IKQAAAQSNF
     ELGHLSKTKA KAIEQACQEI IDGSHYEHFP VDIFQTGSGT SSNMNANEVI ATLASRLGDE
     SIHPNDDVNM GQSSNDVIPT AIALSSAINV VYELLPSLEK LSQHLEHKKA EVGAIVKTGR
     THLMDAMPVT FGQTLSAWQT QINHAAAGIR HSLERVCELA QGGTAVGTGI NADPQFAPLF
     AKNLSANVGI RFTPSSNFFY NIGSQDAIVA LSGQLKVLAV AQMKIANDLR WMNSGPLAGL
     GEIELEALQP GSSIMPGKVN PVIPEAAAMV SAQVIGNDAT ITVAGQAGNF ELNVMLPVIA
     YNILQSIELL ANSAQALGDK AIASFTVNQL NIDKALAKNP ILVTALNPVI GYEKAAKIAK
     QAYKEARPII DVAEQETDLS RSELEKLLNP SKLTQGGL
//

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