ID A0A0Q0VZA2_9BACT Unreviewed; 589 AA.
AC A0A0Q0VZA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=APR54_12970 {ECO:0000313|EMBL:KQC09322.1};
OS Candidatus Cloacimonas sp. SDB.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC09322.1, ECO:0000313|Proteomes:UP000052007};
RN [1] {ECO:0000313|EMBL:KQC09322.1, ECO:0000313|Proteomes:UP000052007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC09322.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) 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}.
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:KQC09322.1}.
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DR EMBL; LKUH01000205; KQC09322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0VZA2; -.
DR Proteomes; UP000052007; 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 4..205
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 589 AA; 64534 MW; 1D52B78C9695569E CRC64;
MFGWMGKIIK IDLTQRIIEN YPVPADWWEK YLGGRGLGVK IYNEICSAQT DPFSAENAVI
FLTGPLTGTV FTSGRYQVVS RSPLTGTICD SSSGGSFGAI LKRTGVDGLI ITGKAEKPVY
LEMVESEIFI KTAEDIWGLN TQQTRDKLTA RLKSGASVAS IGPAGENLVP FAAIMNDKDR
AAGRGGMGAV MGSKNLKAIS VYGTKMTKVH DNEKLKELQV KLDRLIDKNP ITGKSLPLLG
TSVLVNIINA HGMYPTENFK RGVFNDAEGT SGEKITENLL QSKSACFRCP IACGRSTATS
RKSGEGPEYE TVWAFGAQLG VNDLNAITEA NYACNELGLD TITTGSTIGC AMELIEQGAM
DWDLKWGDAA KLVDLVTDIA YKKGWGKDLA LGSKQLAQKY GRPELAMQVK GMELPAYDPR
GVQGQALAYA TSSRGGCHMK AYMISTEILG EPVFMDRFST AGKAEIVTLF QDISAVVDSL
ILCRFIQFAF ATETFCKMLE YVTGIKFDEA KLLEVGKRIY TLERDFNCRA GFTRDDDNLP
SRFLQEKLEE GPSRNRIVEL DSMLTEYYKV RGWNETGIPL EETKKELGI
//
