ID A0A344LJK2_9PSEU Unreviewed; 1137 AA.
AC A0A344LJK2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:AXB48226.1};
GN ORFNames=A4R43_02550 {ECO:0000313|EMBL:AXB48226.1};
OS Amycolatopsis albispora.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB48226.1, ECO:0000313|Proteomes:UP000250434};
RN [1] {ECO:0000313|EMBL:AXB48226.1, ECO:0000313|Proteomes:UP000250434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:AXB48226.1,
RC ECO:0000313|Proteomes:UP000250434};
RA Wang H., Chen S., Wu Q.;
RT "Complete genome sequence and analysis of deep-sea sediment isolate,
RT Amycolatopsis sp. WP1.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP015163; AXB48226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344LJK2; -.
DR KEGG; aab:A4R43_02550; -.
DR Proteomes; UP000250434; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 3.40.50.970; -; 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; 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 Pyruvate {ECO:0000313|EMBL:AXB48226.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 455..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 725..910
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 935..1131
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1137 AA; 120362 MW; 8031E957478B081E CRC64;
MKEAPLTVPT TVTLDDRYAA ERGRALLTGI QALVRLTLEQ RRLDTERGFD TRVFVSGYQG
SPLGGLDSEL VRSKRFLDPA GVVFQPGVNE ELAATAVAGT QTLGQLPGRR HDGVTGFWYG
KNPGLDRAAD AIRHGNLAGT ATLGGAVAII GDDPASKSST VPSSCEPMAQ SLGTPLLAPG
TVGEIIELGL HAVALSRASG LWTGLKIVAD NADASATIDV GGLRLGIPMP PAQPRPTAGA
LVGPAALDAE HDLLTRRLDL ARAYARETGL NRAVFAPAGA RFGVLASGTG FAVLQRALDD
LGLDEAAMEH LGIRLIRLAM PWPIDAEELR RLTADLDEVL VVEDKVPFLE EHLKAALYRV
PGAPLVVGRF DERNRPLLTA RGQLSAEDVA RAVAARAGHE RLPRTATVHL SAIEPRRPAR
IGLPMAGAAR TPYFCSGCPH NTSTRTADGT LVGVGIGCHT MIAIDSTGRG TQIGLTQMGG
EGAQWLGLAP FTDDRHFVQN LGDGTFHHSG SLAIRQAVAG GARMTYKLLY NDAVAMTGGQ
QAIGRLSVPE ITRLLATEGV RRIIVTADDP AKYRGVTLDP IASVRHRDQF AEAEAELAAV
DGVTVLIHDD RCAAEERRLR KRGKLPTPAG KVVINERVCE GCGDCGDQST CLSVQPVATE
FGRKTRIHQP SCNSDFSCLK GDCPSFLLVE PGTVERSVPP LPVALTEPEP RFDDDQTLIR
MPGIGGTGVV TASQILQMAA HLDGRFAAGL EQVGLAQKGG PVVSDIRIAK QPVRGALRAS
RGTADVLIGF DVLGAAEAAN LAVARTGHAV AVLNTAIVPT AAMVSGRVPL PGTADEAVGQ
IADAVGEVVA IDAQSLAEAL FGDHMPTNMV LLGAAYQSGC LPVSAESMEE AIRLNGAAVE
QTLAAFRWGR AAVLDPVAVR EAAQPRVAGS RAEGLDEVLA VRVDDLAGYQ DAVLAGRYAA
EVRRVAALVD GVDPDGRIAV AYARGLHRLL AYKDEYEVAR LHLDPVEKAR RDAEFGPDAK
VSVLLHPPVL RALGMKNKIR LSGRTAEAAF RGLRAMKGLR GTAFDVFGYA KVRRVERRLV
AEYQAFVRAA LERLTAENLD RVVAIVELAE EVKGYEKIKL ATIERFRAKA AEALGAL
//
