ID A0A081MZ13_9GAMM Unreviewed; 1638 AA.
AC A0A081MZ13;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KEQ11436.1};
GN ORFNames=GZ77_25365 {ECO:0000313|EMBL:KEQ11436.1};
OS Endozoicomonas montiporae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ11436.1, ECO:0000313|Proteomes:UP000028006};
RN [1] {ECO:0000313|EMBL:KEQ11436.1, ECO:0000313|Proteomes:UP000028006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ11436.1,
RC ECO:0000313|Proteomes:UP000028006};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEQ11436.1}.
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DR EMBL; JOKG01000007; KEQ11436.1; -; Genomic_DNA.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR Proteomes; UP000028006; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 3.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF13370; Fer4_13; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KEQ11436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028006};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 782..812
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 920..949
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1638 AA; 181575 MW; 5DC4F25EA09E3479 CRC64;
MVKSVEKQFK YPGKRMAIDG NTAVIMCERE ASDAAGAYPI TPSTQMGEYW AEQTAAGHVN
VSGKPLIFVE PESEHAAAAV TAGMSMSGLR ATNFSSAQGI AFMHESLYAA VGKRLPYVLN
VGARAITKAS LNVHCGHDDY HCIDDTGFFQ VFATNAQQAA DLNLIGRKIA ELSLTPAAVA
QDGFLTTHLI EPVMVPERDL VEEFCGCPDD IIECPTPAQK LIYGEKRRRV PELWDVDNPV
VAGTVQNQDA YMQSVAAQRP YFFEHISKIT DECMEEYYQL TGRRYERVMN YKMDDAEYVV
VGQGSMAEQA CAVADYMHEK RGIKMGVVNL TMYRPFPGDL IGKALKGRKG VVVLERTDQP
LAEDLPVIRE IRAAITKCQE NGIAQDETPY EHYATYSKFD TPRLYSGCFG LGSRDLQPEG
IIAAVENMLP EGRHQKFFYL GIDFTREEGL TPKEDIRRQE LLDAYPDIQK MSLKGSENPD
LLPEGAITAR LHSIGGWGMI TTGKNLAVTL FDLLGYDIRA NPKYGSEKKG QPTTYYLSAA
PEPIRINCEY HYVDVVMSPD ANVFGHSNPL FGLKPGGVFI IQSSLETPEE VWATIPRASQ
QYIVDNDINI YYLDGFKIAR EEASNPELQY RMQGNAFQGA FFRASPLLKR GSSSSNGVLT
EDSLFEAIRS QLQSKFGHKG AHVVEDNIRV VRRGFDEMVE ITEKVVGASL PEVRKEEKLP
VMLKQVPVSK DGISDLHKFW DDTASFYAKG DGEGNPADPS LAMSLMPAGT GAYRDMTGIR
FEYPEWIPEN CTACGDCFTI CPDSALPALV NTFGEVFETA INRIETKGMP TRFLRRDTRA
IEKRVRELIE AGGEGSNPNL LIDQAVLEHL SNSTLEGSQK EAQEQEFSLL LDQVSKFDFS
ITKPYYTSRE KKAKGSGGLL SITLNPNTCK GCMECVQVCT DNALVVKPQT DESVEKMRKN
WDFWMDLPTT SEQFSRIDDL DEKVGALETL LMDKANYMST VCGDGACLGC GEKSIIHLMT
STVTAMMQPR IKAHLKEIDD LVARLETHIR MKLAGGVDIS NVDAIEHAIE EHSDHDLTLA
NLTDSLNAEG ASTPIDPKWL RWVTQLVEKL KHLKYRYTEG TTGRGRAAMG ITNSTGCTSV
WGATYPYNPY PFPWANHLFQ DSTSLAMGLF EGHMVKMAEG FKAIRQAKLE LEGKYDSDVH
DKFFTHFKWN DFSDEEYRLC PPVVAIGGDG AMYDIGFQNL SRTMASGVPI KVMVLDTQVY
SNTGGQACTS SFVGQVADMS PYGKAKHGKT EMRKEISLIG MAHRTSFILQ SSAAHTTHLL
EGFIDGFNSR HPALFNIYAA CPVEHGIADD MARHQSKLAV DSRAYPLFRY DPDAGTSYED
CASLEGNAKL TDDWLTYPIK YLDEEGEQKT MELPFTFADF AMTEGRFSKH FRKVPQDAWN
DEMVPLHEFL GMDNSDREGL FPYVMATDSK NHLVRVLVAQ EMVNSCDERR HFWRQLRSLT
GVENQAKVKA AATEAKAELA SQLTGKIEEL VGTITVSPTI AAPAAQGDNL IPAVQVGEGV
WVESAECTAC DECINIAPGV FAYDSDGKVQ ITNPQGAAFK DIVKAAEKCT AGSIHPGIPW
DQSEKDLDKL IKRAEKFQ
//
