ID H0UR00_9BACT Unreviewed; 731 AA.
AC H0UR00;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:EHM09829.1};
GN ORFNames=TheveDRAFT_0670 {ECO:0000313|EMBL:EHM09829.1};
OS Thermanaerovibrio velox DSM 12556.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=926567 {ECO:0000313|EMBL:EHM09829.1};
RN [1] {ECO:0000313|EMBL:EHM09829.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12556 {ECO:0000313|EMBL:EHM09829.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Noncontiguous Finished genome of Thermanaerovibrio velox DSM 12556.";
RL Submitted (OCT-2011) 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; CM001377; EHM09829.1; -; Genomic_DNA.
DR RefSeq; WP_006583323.1; NZ_CM001377.1.
DR AlphaFoldDB; H0UR00; -.
DR STRING; 926567.TheveDRAFT_0670; -.
DR eggNOG; COG2414; Bacteria.
DR HOGENOM; CLU_020364_1_0_0; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000005730; 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:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE: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 21..248
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 731 AA; 82980 MW; 80BFAE24F208C077 CRC64;
MEKMKLLAQW TYTPKPIHRG YTKEVCFVDL GNRDGKYSFK TKPLSDEFVE RFTGGRGFGL
GLLWEAVNEN TKWDDPENEI IISGGPLCGI TQYPGAGKCY SVFLSPATKQ TYASNAGGYF
GPLIKFSGFD SFELRGIADK NVIIFVDGDL GKVEIYESPF DDKSNSYTIT DELHEYFSAE
DEDRENGKRA ISVVSTGQAA HHSYICGMNF SFYDLRRKVA RLKQAGRGGG GTVLRHKGVH
AIVVKKRKVT GVENDPADLA TLQKVGIKLH KEIHDYDDVQ CKMRKVGTAH LNEVMNDYHL
LPVNNYKFGQ HPDINNIHSD VYTSLFTQGL PDGCWYGCSL SCAKAADHFE LKTGPWKGRK
VTVDGPEYET AASLGSVIGI FDPKWTIEAN FYADHYGFDT ISLGTIIAFL AECYELGLIN
DEHTGGLKLN FGNKEHMMEL IHRMAEGKDE FAVAASRGIR YLKDFLSEKY GADRKIMEDI
GMEGQGLEVS QYRCQESIAQ WGGYFLTLKG PQHDEAWLIF MDMVNKQLPT FEDKAEALYY
FPNFRLWFSL VGLCKLPWND IEPADNHVKY KGIEAAKVPE HVQNYVDIFN AVTGKNITKE
DIITQSERVY NFERVFNLRL GKGTREWHNI PARGLGPVFE DEYMARPDYF DDKLREAGIN
PEGLSVKEKI EKLQAYRRGQ WEQLVDAVYK RRGWNKNGIP TLETVKRLGI DTPEVVEVLK
KHLRPEDEWD N
//
