ID A0A0S7WMB9_9CHLR Unreviewed; 617 AA.
AC A0A0S7WMB9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=AMJ38_00830 {ECO:0000313|EMBL:KPJ51326.1};
OS Dehalococcoidia bacterium DG_22.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ51326.1, ECO:0000313|Proteomes:UP000054105};
RN [1] {ECO:0000313|EMBL:KPJ51326.1, ECO:0000313|Proteomes:UP000054105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_22 {ECO:0000313|EMBL:KPJ51326.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ51326.1}.
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DR EMBL; LIZQ01000013; KPJ51326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WMB9; -.
DR PATRIC; fig|1703393.3.peg.1240; -.
DR Proteomes; UP000054105; 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}.
FT DOMAIN 6..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 617 AA; 66361 MW; E6B75358A37FD6FB CRC64;
MLNEAINGKI LTVNLSSGAS ESESLPEEVY RRYIGGYGLG VRLLFDRIPH GAEALGPDNI
LGFFPGLLTG TPLFGSRYQA VGKSPKTGGW GDANSGGDFG PFLKHAGWDG LLFSGISDRP
VYLLIEDGKV EIKDASDLWG LDAITTEAEL KERHGKKASI ACIGQAGEKL SYMAGICNEY
GRLAARSGLG AVMGSKRLKA VVVLASRNIL AGDDKNVRSL VRTSIDEFGP IAAFFRGFGT
TGVTATSAVT GDSPVKNWGG VGTVDFPAAS QLAGDKFNAK MDKTYACWHC ALSCGAESKE
SDNPRFPYPK GTHRAEYETA CAFGTLALNA DIDSLQCVNH LCNAYGLDSI SAGATVAFAI
ECYENGLISN EDTGGLELTW GNGEAIVEMV HRIGKREGVG DLFGDGIRKA AEKLGAKAEP
FAMEVGGEEL PMHEARLQPE YFVAYKLDPT PARHTQYPSS IAPDWGVPPA PGDRNQASGR
AQHHKGMSEC QHIVNSIGTC MFITFAGPDQ RIPEWINAVT GWDITHQELL KTGERIANLR
MAFQVREGDN PAQRRIPGRL IGSPPLEEGP HKGFSLDAET LQREFLAACD WDQQTCKPSR
AKLEELGLED VADVLYE
//
