ID A0A0S7ZTC1_9GAMM Unreviewed; 587 AA.
AC A0A0S7ZTC1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:KPJ90292.1};
GN ORFNames=AMJ53_14025 {ECO:0000313|EMBL:KPJ90292.1};
OS Gammaproteobacteria bacterium SG8_11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703402 {ECO:0000313|EMBL:KPJ90292.1, ECO:0000313|Proteomes:UP000051175};
RN [1] {ECO:0000313|EMBL:KPJ90292.1, ECO:0000313|Proteomes:UP000051175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_11 {ECO:0000313|EMBL:KPJ90292.1};
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:KPJ90292.1}.
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DR EMBL; LJNJ01000303; KPJ90292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZTC1; -.
DR PATRIC; fig|1703402.3.peg.1774; -.
DR Proteomes; UP000051175; 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 1..213
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 587 AA; 63037 MW; 017BC028AA671747 CRC64;
MWILRINMTD QSYKLEELPE KYKHLAGRGF TSTLIHDEVP PTAHPLGPNN KLIFSPGFVT
GTPAPTSARI SCGAKSPLTG GIKESNAGSE WPDALASMQI RGLVVEGKPV QNGKFWVALL
SWDKDQEKPK VEFSPADEYV GLTAQESFNK VYTNFGKKVT VAGIAASGEI LNSNSGIVFD
DLEHRATRYA GRGGLGAVMG SKGLKYIVID RKGAPGKEIA DKALFNEGRK KLTDSLRTHD
ITKPKGGLNT HGTAVLINVM NEAGGLPTRN FSSGRFEGAP NISGEAVFDG NKERLGKELY
NHACSPGCII QCSNTWHHED GTEHVSCFEY ESSWSLGANC GIDDIDDVAE LIRLCNEYGY
DTIETGTTLA VAMEAGIAEF GDGKRAIELL HEMGKGTPLG RILGAGTNYA AQVLGVVHNP
TVKGQSMPAY EPRAVKGIGI TYATTPMGAD HTAGYTIAPE ILGVSGSADP LSPEGKADLS
RAFQASTAFI DSSGHCLFIA FAILDIETGF QGMIDEVNGV LGTNFTADDI LEMGKDILRK
ERAFNEAAGI TKAHDRLPEF MKYEKLPPHD HVFDVPDEAL DAVFAEL
//
