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Database: UniProt
Entry: A0A437QCZ0_9GAMM
LinkDB: A0A437QCZ0_9GAMM
Original site: A0A437QCZ0_9GAMM 
ID   A0A437QCZ0_9GAMM        Unreviewed;      1159 AA.
AC   A0A437QCZ0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase family protein {ECO:0000313|EMBL:RVU32396.1};
GN   ORFNames=EOE65_01715 {ECO:0000313|EMBL:RVU32396.1};
OS   Neptunomonas marina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptunomonas.
OX   NCBI_TaxID=1815562 {ECO:0000313|EMBL:RVU32396.1, ECO:0000313|Proteomes:UP000282818};
RN   [1] {ECO:0000313|EMBL:RVU32396.1, ECO:0000313|Proteomes:UP000282818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPM-16 {ECO:0000313|EMBL:RVU32396.1,
RC   ECO:0000313|Proteomes:UP000282818};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVU32396.1}.
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DR   EMBL; SACQ01000001; RVU32396.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437QCZ0; -.
DR   Proteomes; UP000282818; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:RVU32396.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282818}.
FT   DOMAIN          738..924
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          951..1148
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1159 AA;  127185 MW;  ED8D0CF8DBBF37D3 CRC64;
     MTRATYAPAA GSTAPLDTYE LDERYTRTEG RVFLTGTQAL VRLPLVQARL DQQNGLNTAG
     FISGYRGSPL GGYDQALWSA KKHLESHNVE FVPAINEDLA ATLVLGSQQV ETDPDKQVDG
     VFSIWYGKGP GVDRAGDALK HGNTYGSSPN GGVLVVAGDD HGCVSSSMPH QSDVAFMAWF
     MPTINPASIA EYEAFGLWGY ALSRFSGTWV GFKAISETVE SAASVELKPL PNFVTPTDFT
     PPDSGLHYRW PDLPGPQLET RIEHKLAAVQ AFARANPIDT KVLSCDNPTL GIITTGKAHL
     DLMEALDLLG LDGQTLQTLG VEIYKIGLVW PIERHGVLDF VHGKREILVV EEKRGIIESQ
     IKEAMSEPDH PGEVLITGKQ DEAGEPLIPY VGELSPSLLA RFIVARFTRL FDIDLTEPLS
     AITESGVAVK DPGGVRRLPY FCSGCPHNSS TKVPEGSKAL AGIGCHFMAS WMGRDTESLI
     QMGGEGVNWA SKSIFTGKGH IFQNLGEGTY FHSGSMAIRQ SIAAGANITY KILFNDAVAM
     TGGQPVDGQI TVPAIAQQVS AEGVKKVVVI SDEPEKYRGH ESQFPSDVTF HHRDELDDIQ
     RMLRDIPGVT VLIYDQTCAA EKRRRRKRGQ FPDPAKRVMI NHHVCEACGD CSVQSNCLSI
     VPRKTELGVK RQVDQSSCNK DYSCVNGFCP SFVTIEGGEL RKPEAKGTAQ LDAKLEHLST
     PEFKPLANGY DLLVSGVGGT GVVTVGALIT MAAHLEGKGA SVLDFMGFAQ KGGAVLSYIR
     LSEQPSALNQ VRIDHGRADA LIACDMVVAS SAKALDVLRH NHTQAVINEA EMATADHVLY
     RDADIESGKR IDLITEAVGS AQCDHFNANE LALSLLGDTV FSNVMMLGYA WQKGLVPVSL
     AALERAIELN RVAVEKNLNA FKWGRLLAED PKAAQFALTP SEPVKLIATL DQQIDRFADY
     LIQYQDAAYA DQYRALVASV RAKEQQLTPA SDTLSRTVAK QLFRLMAYKD EYEVARLYTE
     TDFLKEVEAT FTGDYQIHFN LAPPLLNKTQ RNGRPKKRQF GPWMLKSLRM LAKMRKVRHT
     VLDPFRFSAD RRLDRQLLEN YKRDITTWVA ELNSHNLTTA IEIARLPEEV RGFGPVRDAA
     AEQAEQQREI LFVQFKQAK
//
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