ID A0A2H3KT68_9CHLR Unreviewed; 604 AA.
AC A0A2H3KT68;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:PDV98469.1};
GN ORFNames=A9Q02_15315 {ECO:0000313|EMBL:PDV98469.1};
OS Candidatus Chloroploca asiatica.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Candidatus Chloroploca.
OX NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV98469.1, ECO:0000313|Proteomes:UP000220922};
RN [1] {ECO:0000313|EMBL:PDV98469.1, ECO:0000313|Proteomes:UP000220922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7-9 {ECO:0000313|EMBL:PDV98469.1,
RC ECO:0000313|Proteomes:UP000220922};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:PDV98469.1}.
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DR EMBL; LYXE01000099; PDV98469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3KT68; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000220922; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000220922}.
FT DOMAIN 5..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 604 AA; 65553 MW; 310F75BB5F57E657 CRC64;
MLGGFANRIA HVDLTHRTVE YRAIPDDWAR LYIGARGLAV RYLFENGPQV EPFSPENMLC
FMNGPLTGTD ANMSGRQAVV TKSPLTGTVT DSHIGGWSAA RMRWAGFDGL VITGKADAPV
YLYLENGEVS IRDASDLWGK GIHTVIPMLK ERYGEKDLSV MAIGQSGENL IRYAGWVNEN
DRAAGRGGTG AVGGSKQLKA IVIKAARAIP KADDREAWKV AHKRALATIM DEKNITSPRK
GGLSVYGTNV LMNITNTMGA LPAFNSQKTS FGSRAELISG EYVNDNILVD NPTCHACPVA
CKKEVEIKEG PWKGLRMESV EYEPAWAVGA NCGLDDINTV AKLIDLCNDH GMDPIELGNV
FSCYMECCER GYANGGGPLL WGDAMAMVEM TTKIALREGV GDILAEGTAR VAAHFNHPEL
SMTVKGQAIP AYDPRGLKGM GIAYATSNRG ACHLRAYTPA SELGVIPLKT DPLAWQGKGE
LTKLFQDLHA FSDSLDLCKF SAFAEGAEEY AAQYSAYAGI PFTVEDVLVA GERIYNLERR
FNNLAGIAEG SDYLPDRFTK EPSTMPGSEG HVCELDLMLE EYYTARGWVN GVVPEAKLQQ
LQVV
//
