ID A8MK89_ALKOO Unreviewed; 599 AA.
AC A8MK89;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN OrderedLocusNames=Clos_2690 {ECO:0000313|EMBL:ABW20221.1};
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW20221.1, ECO:0000313|Proteomes:UP000000269};
RN [1] {ECO:0000313|Proteomes:UP000000269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + dihydrourocanate = AH2 + urocanate; Xref=Rhea:RHEA:36059,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:27247,
CC ChEBI:CHEBI:72991; EC=1.3.99.33;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU366062};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|RuleBase:RU366062};
CC Note=Binds 1 FMN covalently per subunit.
CC {ECO:0000256|RuleBase:RU366062};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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DR EMBL; CP000853; ABW20221.1; -; Genomic_DNA.
DR RefSeq; WP_012160528.1; NC_009922.1.
DR AlphaFoldDB; A8MK89; -.
DR STRING; 350688.Clos_2690; -.
DR KEGG; aoe:Clos_2690; -.
DR eggNOG; COG1053; Bacteria.
DR eggNOG; COG3976; Bacteria.
DR HOGENOM; CLU_011398_4_0_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000000269; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1010.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR SMART; SM00900; FMN_bind; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366062};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366062};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366062};
KW Reference proteome {ECO:0000313|Proteomes:UP000000269};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 31..599
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022262632"
FT DOMAIN 50..124
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 599 AA; 63890 MW; 7D7D08DCB0FE48C2 CRC64;
MNQIKVIRNI MCVILCVIML LSMVACQPKA VDLTETDMFK AGTYTSTAKG HSGDIKVEVV
VDENSIKDVK ILEHIESPSI SDPAIERIPK AIVDGQTLAV DTISGATVTS KAIIVAVTEA
LKQAGGDIDL LSVKKENTKT LGETVEYTTD VIVIGGGGAG LAAAVSAHQN GAAVMVVEKM
PRLGGNTIIS GSAYNAVDPK RQSAQGIEDS IEKHIKQTYE GGDKQGNLAL IETLVENAYP
AIEWLESLGM EFKEDIFTVL GGLWPRAHKP VKPLGTGFIS TYENYINENE GVTVLLDTEI
TELIVDNNRV VGVKGKGLEG EVIINANNGV IIATGGFGAN IAMRDQYNTN WPSLTNIKTT
NHPGATGDGL TLAEKIGASL VGLENIQLLP MGDPETGSLS GNIEQGVENR IFVNKDGNRF
VDEGERRDVM TKALMEQKDA AMWVIVDKNS YPTGETKNNF NESIDELVSQ NRAFKADTLE
DLAKQIGVNP DNFVKAVKEF NEAVDGTPDK FGRTLFDKKI DTAPFYAGAR VPTVHHTMGG
IEINTSAQVL DKDGNIIHGL YAAGEVTGGI HGANRLGGNA LADITVYGKI AGESAAAKK
//
