ID A0A0U5H533_9EURY Unreviewed; 643 AA.
AC A0A0U5H533;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN Name=aor2 {ECO:0000313|EMBL:CQH58404.1};
GN ORFNames=HHUB_2743 {ECO:0000313|EMBL:CQH58404.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH58404.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001714};
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; LN831302; CQH58404.1; -; Genomic_DNA.
DR RefSeq; WP_059057163.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5H533; -.
DR STRING; 1407499.HHUB_2743; -.
DR GeneID; 26659373; -.
DR KEGG; hhb:Hhub_2743; -.
DR OrthoDB; 30771at2157; -.
DR Proteomes; UP000066737; Chromosome I.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:CQH58404.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066737}.
FT DOMAIN 7..212
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 266..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 69195 MW; F99BEA36F951C27D CRC64;
MTDLGGYQDN VARVDLSAGD VDYESIDDED AREYIGGRGL GVKYVFENGP DVEPLSEENL
LAFMTGPLTG TQTPMSGRIA VVTKSPLTGT VTDSHHGGWS GARLKWAGFD GLLFEGKADD
PVYAVVEDGE LELRDASHLW GQGIHGTLDD LEEEVEGSYG KNLSAMTIGP GGENEVRYGC
IINEDDRASG RGGTGAVMGS KNLKAVVVKA GTDMPKPADR ETFMEGHKAA MQAIQESDVT
APNEGGLSVY GTNVLMNLTE EMEGLPTRNG RFTSTTTEAD AEPDEPNIDS EKVSGENVEE
NILVDDPTCH SCPVACKKEV EVDVNHKGED LNVRMESYEY EPAWALGPNS MNDDRDMIAV
MMDRCNDLGI DSIETGNLLA FAMEATEKGY IDGEGIDWGD LDAMTEMIEK IGEREGDLAN
TLAEGQKRAA EELGAHDCRL DVKGQSIAAY DPRGLKGMGI GYATSNRGGC HLRGYTPAAE
ILGVPEKVDP TDWEGKGELT ATFQDLHAIS DSFDICKFNA FAEGVQEYIA QYNGMTGRDV
GEEDLLEVGE RIYNLERYYN NLAGFDGDDD TLPDRFVEGA EDAVPAGGGI EGELCELDKM
KDEYYRDRGW VDGVVPDEKL DDLGIDFGPG TGVSAGGAAS ADD
//
