ID A0A080M3W3_9PROT Unreviewed; 615 AA.
AC A0A080M3W3;
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=Putative oxidoreductase YdhV {ECO:0000313|EMBL:KFB75060.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KFB75060.1};
GN Name=ydhV {ECO:0000313|EMBL:KFB75060.1};
GN ORFNames=AW06_003915 {ECO:0000313|EMBL:KFB75060.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB75060.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB75060.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the AOR/FOR family.
CC {ECO:0000256|ARBA:ARBA00011032}.
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:KFB75060.1}.
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DR EMBL; JDST02000107; KFB75060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M3W3; -.
DR STRING; 1453999.AW06_003915; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR PANTHER; PTHR30038:SF0; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 ECO:0000313|EMBL:KFB75060.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315}.
FT DOMAIN 3..206
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 615 AA; 65917 MW; 8C0DDDE4D527C444 CRC64;
MAWTRKILRV NLTQGTCSSE PLNMAWAAQY LGQRGLASKY LVSEIDPQVD PLSPENKLIY
ATGPLTGTMA STGGRYSVIT KGPLTGAIAC SNSGGYFGAE LKSAGWDMII FEGKSPQPVY
LHIENQQATL LPADDLWGKT VWDTEGTLKK RHQDSLLRVS SIGRAGENQV LFAAIVNDLH
RAAGRSGVGA VMGSKNLKAV AVRGTLGVGN IADPKAFMAA VTAGKKVLAE NAVTGQGLPT
YGTQVLMNVI NEMGASPTRN HRDVQFEGAR KISAEAMHEK RATDGRTHLV TNQACFGCTI
ACGRISRIDE THFSVQTKPE YWGANGGLEY ESAWALGNAN GVDDLEALQY ANLLCNEDGM
DPISFGATVG AVMELFELGI LTREDIGLDA PFGSAAALCR LAEMTVRGEG FGKIVGQGSK
RLCTQYGRPE LSMTVKGQEF PAYDGRALQG MGLAYATSNR GACHLRGYVV SSEVFGIPVK
TDPRDTDGKP ELLKAFQDAT AIVDSSGLCV FTTFAWTLND IQPQIQAACP GDWSLESLLA
MGERIWNLER DFNLAAGLSS KDDTLPPRLL TEPCKTGASK GMVAELGKML PEYYRLRGWT
PDGVPTTATR ARLGL
//
