ID A0A1F8LZN4_9CHLR Unreviewed; 637 AA.
AC A0A1F8LZN4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=A2Z70_00490 {ECO:0000313|EMBL:OGN91795.1};
OS Chloroflexi bacterium RBG_13_48_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797621 {ECO:0000313|EMBL:OGN91795.1, ECO:0000313|Proteomes:UP000180319};
RN [1] {ECO:0000313|EMBL:OGN91795.1, ECO:0000313|Proteomes:UP000180319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN91795.1}.
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DR EMBL; MGMO01000024; OGN91795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8LZN4; -.
DR Proteomes; UP000180319; 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..206
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 637 AA; 70738 MW; E770F712D57EFE1B CRC64;
MHGWAGKILQ VNLTDSEIST ISTRPYAEQY LGGRGIASRL YWETVAPGIT AFDPENRLIF
MTGTLVATGA QGASRLSIVG KSPMTLPEGY CYGNMGGFFG AELKKAGFDG LIISGCAPHP
VYIWINDNEV EIKDASSLWG KNAYRTGEML QHIHGDNVRF VTTGVAGERL VRTAIAFASH
QSTSTAGFGA VMGSKNLKAI AVKGTGKPSV AYPEKLKELN QYTVKICKRC TLVAPPVVMA
TGRGHLVEVI GKGRCYQCGL ECNKQLYRYG QRLEGYRRCQ SMEYYLPWKY SQEDEPVDTF
FDAPTLANDY SIDTFELQSM IDWLYACYKA GSLTNKETDL PLSKIGTRSF LEKLLHLITY
REGFGDILAE GLVRAGDKVP EKARAMFSHV IAPICMHDLV PPRAIVAHAL LYPMEPRVHQ
PIIHEINFVR IAWALNQCQP PATPVTTEVF RKVAKAFWGS EEASYVSTYE GKALAAMKVQ
NRTYAKDSLG LCDFSWPISY SFATPDYMGD PDLEAKIFNA VTGVAVEEVD RCSERMFNLQ
RAILLREGWK VPKADYPPEF NFTEPLQTDP HGMNLLVPSP EGGAKDAAGN ILDRDKFTVM
LKEYYRLRGW NEETGLPHAE TLIALGLDDL VPFCQSQ
//
