ID A0LQP2_SYNFM Unreviewed; 578 AA.
AC A0LQP2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ABK19744.1};
GN OrderedLocusNames=Sfum_4079 {ECO:0000313|EMBL:ABK19744.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK19744.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK19744.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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}.
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DR EMBL; CP000478; ABK19744.1; -; Genomic_DNA.
DR RefSeq; WP_011700857.1; NC_008554.1.
DR AlphaFoldDB; A0LQP2; -.
DR STRING; 335543.Sfum_4079; -.
DR KEGG; sfu:Sfum_4079; -.
DR eggNOG; COG2414; Bacteria.
DR HOGENOM; CLU_020364_1_0_7; -.
DR InParanoid; A0LQP2; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000001784; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT DOMAIN 1..209
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 61107 MW; A4BB65CD6C8F806D CRC64;
MNKILRIDTG AEGGPQATVG SPGEYAGLGG RALTSTVVAR EVPPLCHPLS AENKLVIAPG
LLSGTSGAMS GRISIGAKSP LTGTIKESNA GGQPSQVLAR LGYAAVILEG KPATDDLYKV
VIDKEGVRIV RDNSLRMLPN YDLIEKMKSE HGEHIACISI GPAGEMKLGA ASIACTDTEL
RPTRHAGRGG LGAVMGSKGI KVIVLDDSGM KTRQPKDPDK FHAANKKFVE GLRNHPVTGQ
GLPAYGTNVL TNIINEAGGY PTCNFRQGRF EKAHQISGET QAETETVRGG LATHGCHRGC
VIRCSGIYND KDGRYLTKQP EYETVWAHGG QCGISDLDAI AMLDFLDDNY GLDTIEMGVA
LGVAMEGGLL RFGDAEGAVN LVKEVGKGTP LGRILGSGAE ITGKAFGVAR IPVVKGQALP
AYDPRAVQGI GVTYATSTMG ADHTAGYAVA TNILKVGGDV DPLKPEGQIE LSRNLQIATA
AVDSTGMCLF IAFAVLDQPD TFQALIDMIN AFYGLQMTAD DVVALGKQVL KTERDFNARA
GFTAQHDRLP RFFKTEPVGP HNVTFSVPDE ELDRVHDY
//
