ID A0A2S7K5A7_9PROT Unreviewed; 1152 AA.
AC A0A2S7K5A7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:PQA87695.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:PQA87695.1};
GN ORFNames=CW354_04835 {ECO:0000313|EMBL:PQA87695.1};
OS Marinicaulis flavus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Marinicaulis.
OX NCBI_TaxID=2058213 {ECO:0000313|EMBL:PQA87695.1, ECO:0000313|Proteomes:UP000239504};
RN [1] {ECO:0000313|EMBL:PQA87695.1, ECO:0000313|Proteomes:UP000239504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY-3-19 {ECO:0000313|EMBL:PQA87695.1,
RC ECO:0000313|Proteomes:UP000239504};
RA Hurst M.R.H.;
RL Submitted (DEC-2017) 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:PQA87695.1}.
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DR EMBL; PJCH01000005; PQA87695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7K5A7; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000239504; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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.
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:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PQA87695.1}; Pyruvate {ECO:0000313|EMBL:PQA87695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239504};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 453..601
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 726..913
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 945..1144
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1152 AA; 125910 MW; 8861EF72B6A3487A CRC64;
MKNAAISLED KYTLREGRVF VTGTQALVRL ALMQRWRDEA ASLNTAGFVT GYRGSPLGSV
DQAFARAKKF ADDADIRFHP GVNEDLAATS VLGTQQINLH ETAKKQGVFS IWYGKGPGVD
RSGDAFRHGN LAGSAHHGGV LILAGDDHTC KSSTTSHQSE YALMDAMIPI LNPAGVQDIL
DFGLFGWALS RYAGTWAAMK LVADTMDSSA SVQVSDSRIA VGLSVDFDMP SGGLSIRWPD
TPQEMERRLH NFKIPAALAF ARANRLDRVT LGGVRRQLGI VTTGKSYLDV LQALEALGID
QQRAAELGLS IYKVGMVWPL EPEGIKTFAT GLQDLLVIEE KRPLLESQIK DILFGLPADQ
RPRVFGKKDE HGRIVLPAHD DLSSSLIAKV IAERFMPWLQ DTEFAKRARQ AIASAAALSQ
SAPLVERTPY FCSGCPHNSS TKVPTGSRAL AGIGCHYLVL RMDRDTATFT HMGGEGANWI
GQAPYVPTEH VFQNLGDGTY FHSGLLAIRA AVAAKVNITY KILFNDAVAM TGGQAHDGQI
SPQRISHQVR AEGVERIAIV SDDIQKYADQ PAFVGNVSIH HRSELDAVQR ELREHRGVSV
LIYDQVCAAE KRRRGKRSAA KPVTNRHLFI NELVCEGCGD CSKKSNCLSV TPIDTEYGRK
RRIDQSTCNT DFSCLEGFCP SFVGVEGASL RKPEATDLES LLAVDLHQPQ IRRLDQPWNI
LITGVGGTGI ITIGAIVTMA AHIEGKGCTT LDMTGMAQKG GPVTSHIRLA ASPEDIHASR
IATGAADLLI GGDLVVTTSR EALDVINKGT THVVLNQQQT ITADFIRDRN FNVPADRLVG
AVSATAGAGK VDLVAATKIA EKLLGDSIGA NLFLVGYAFQ RGLIPVEEGS IQTAIKLNRV
AVEMNTTAFR LGRLAAQRPD LFKQVDAQQP GLAAIDHRAP STSIEETISR RVAFLTDYQA
KWYAQRYESF LTKVRAREVE VMGREGSFSE AVARGLFKLM AYKDEYEVAR LYSGKAFREM
LSETFVDGGR LSVHLAPPLF ARKDPTTGIP RKMAFGPWAF KMFAALARMR RLRGTPFDPF
GYTAERRTER QLILDYMDSI GRLLQDLTPA RVPHAIEIAS LPDDIAGFGH VKAESVRKAK
IRWRLLEGKR CF
//
