ID A8MAS5_CALMQ Unreviewed; 629 AA.
AC A8MAS5;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ABW01111.1};
GN OrderedLocusNames=Cmaq_0263 {ECO:0000313|EMBL:ABW01111.1};
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW01111.1, ECO:0000313|Proteomes:UP000001137};
RN [1] {ECO:0000313|EMBL:ABW01111.1, ECO:0000313|Proteomes:UP000001137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC {ECO:0000313|Proteomes:UP000001137};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AOR/FOR family.
CC {ECO:0000256|ARBA:ARBA00011032}.
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DR EMBL; CP000852; ABW01111.1; -; Genomic_DNA.
DR AlphaFoldDB; A8MAS5; -.
DR STRING; 397948.Cmaq_0263; -.
DR KEGG; cma:Cmaq_0263; -.
DR eggNOG; arCOG05072; Archaea.
DR HOGENOM; CLU_440510_0_0_2; -.
DR Proteomes; UP000001137; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001137}.
FT DOMAIN 3..218
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 629 AA; 70234 MW; 9001FAD1936B36DB CRC64;
MKHMKVLNVD LTSGSVSITS VEAQGPVTLG VRILSNEDTY SKDPLDPSVP FIIGIGPFVG
GKLPGVHRAI AVFKSPMTKT IHVAAIGGVA YKFMGSGIDA VVVRGRSGKP TALFISSDGV
EVRQVNPVYS YSGLNGVYAF TKYLMDSFND FFTKYNARAI VVGEAALKTY NGALFSIDVD
PRRREFKPGA EDTAARGGPG TVMAQGHNLV AIVAGGSVKA RYVKVTDMNL INKMSMESFK
KPFIQVMGEK TIKYRYDPSM GTGGTFGVNY PHYRELLPLF GYKSIYMPRD IRVKHVEAII
NLFWKPFNDE VFVKSKSWYN CGDFGCSVVC KKVWRGKKVD YEPFHAAGPF IGNYIFQEAV
KVVDLIDEYG FDAIEMGHVI AWVFDSIENG LLKPEEVGLS DKPIFNPYEF APERDSLRNA
KLAGELINGL VNKSTPILRM IAENGIRVSA RRLNEMFSDR VKATGKSFND LVVYVAYGES
GYMTPNFYWT PGMVAPMYIL GRYWTNYSNT FMKPEDYAKS ALERAINEAL IDDAGICRFH
RGWAEPMLEK MYSEFTGMKP NKNLYRELAE YSIKAGAQPK PWESSRAADV VATLAKEIGS
KEWVFESKSD YTEWWIRYKV ALDKQLGVA
//
