ID   A0A109UL51_9GAMM        Unreviewed;      1085 AA.
AC   A0A109UL51;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Putative FAD-linked oxidoreductase {ECO:0000313|EMBL:AMC99988.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:AMC99988.1};
GN   ORFNames=LOKO_00907 {ECO:0000313|EMBL:AMC99988.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMC99988.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMC99988.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMC99988.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT   Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMC99988.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMC99988.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP014226; AMC99988.1; -; Genomic_DNA.
DR   RefSeq; WP_066445615.1; NZ_CP014226.1.
DR   AlphaFoldDB; A0A109UL51; -.
DR   STRING; 507626.LOKO_00907; -.
DR   KEGG; hco:LOKO_00907; -.
DR   PATRIC; fig|507626.3.peg.901; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000063387; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:AMC99988.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387}.
FT   DOMAIN          53..285
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          719..749
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1085 AA;  118697 MW;  97E0E7B26526237D CRC64;
     MISRLDTAQS STLAGLDARY LRFLDVLKAR GFEGDIAPDY ASRTVQATDN SIYQRLPQAV
     LFPRHAADLE LIARLAGEAA HRQVVLTPRG GGTGTNGQSL TDGLVVDVSR HMNQILEIDV
     ENRRARVQAG VVKDQLNAAL RPHGLFFAPD LSTSNRATIG GMISTDASGQ GSCEYGKTRD
     HVLELDTLLL GGERLLSRPI AEAELETLCH HSGVIGNAYR TAREIIDDQG KLIAAKFPPL
     NRCLTGYDLA HLRDAEGRLD MNSLLCGSEG SLGFLNEAVL NVLPIPKHST LVNVRYAGFM
     DALRDAKALM ASAAKPTSIE TVDDKVLTLA MEDFVWDSVA EFFPSADSAK DSNTATATQQ
     AAAIRGINLV EFNDDDPKRL TERVAAFCRH LEADASVPRL GYTLAEGRPQ IQKVYGMRKR
     AVGLLGNARV DEKGEKRPIP FVEDTAVPPE RLADYIAEFR VLLDARGLAY GMFGHVDAGV
     LHVRPAIDMK DPVQEQLIRE ISDEVAELTH KYGGLLWGEH GKGVRSEYAP KFFGELYPSL
     QRVKAAFDPH NQLNPGKIAT PMLIPPEPAG MALDTPAEPS EEAFDISPEA VEAQPVNLID
     PGLLTIDGVP TRGQLDRQID ERVWQSHAAT VYCNGNGACY NYDPNDAMCP SWKATRDRVH
     SPKGRASLIR EWLRLQGNAG IDLVEQAHQQ RAEGSLGFLK RLPARIRNTV KRREEADFSH
     EVYDAMAGCL ACKSCAGQCP VKVNVPESRS LFLEAYHARY LRPVRDYLIG GLEFFAPALA
     SVAPLYNAAL NTRLVERLLA GPIGMVDSPR LSRARLKQQL AAWGISEATP ISLGLLTEAQ
     KARSVVIVQD AFTSFFEADV ALDIVELLSR LDIRVFVAPY SPNGKPLNVQ GFMGAFTRTA
     EKQARRLRAL AEFGVQLVGI DPAMTLTYRQ EYVKALAPDS VPEVLMLQEW LVAQGQRLVP
     PGLSQQLEAL ADPGYRLLSH CTEKSNAPGS PKAWQQVFAA FGFELELLST GCCGMSGTYG
     HEARNLETSK TIYAQSWQPV VEGEASPGRL LATGYSCRSQ AKRLSDTGLP HPLQGLLNQL
     RQLSW
//