ID A5CY57_PELTS Unreviewed; 631 AA.
AC A5CY57;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:BAF61078.1};
GN OrderedLocusNames=PTH_2897 {ECO:0000313|EMBL:BAF61078.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF61078.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF61078.1; -; Genomic_DNA.
DR AlphaFoldDB; A5CY57; -.
DR STRING; 370438.PTH_2897; -.
DR KEGG; pth:PTH_2897; -.
DR eggNOG; COG2414; Bacteria.
DR HOGENOM; CLU_020364_1_0_9; -.
DR Proteomes; UP000006556; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556}.
FT DOMAIN 4..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 631 AA; 68899 MW; D41C036216E77B70 CRC64;
MGGYAGRILL VNLSTAEILV ERPAEEFYRK YLGGPGIGLY YLLKNNRHYF DPFLPESIMV
FAPGLLTGTS APCVPRYTVV ARSPLTGALG KSEAGGWWGP ELKKAGFDAV VISGRAPRPV
YLWIKEGEAE IRDASRYWGL ETGDVQEGIR RELGDSRVQV AQIGPAGENL VRYANICNNL
AHFNGRNGLG AVMGSKNLKA IAVRGSRTVE VKDQDRVKEI LRWVTGQVKV HPLSAALHEH
GTPMGVTGNN AGGVLPTNNF DTGVFGRAEE IGSEKLNAHY LVRRGGCFAC PVKCKRIVEV
RDGDMVVDRK YGGPEYEALA ALGSNCGIGN LKLLLKANEL CNRYGIDTIS LGMSLSFAMK
CYEEGIIGKE QTGGLELRFG NEDVLLPVIE KVARRDGFGN VLADGSRAAA ARFGKASEKF
LVEVKGQEVP MHDPRVKSGV GLQYALSVNG ADHWFAQHDP FFTGKDGFGV KGGAPIGLGE
PVEAEDLSHR KVRQVLYTSY LNGAYDLLGA CVFGFVARSL TPLDKLLELV EAVTGWKTSW
WELLKAGERY LAMAKEYNAR QGLTINDDYL PEKFFAPLKG GPVDGKPGLD REKFKEAVRL
FYEMAGWDGD TGRPLAAKLY ELDLDWLVEK G
//
