ID C5C705_MICLC Unreviewed; 389 AA.
AC C5C705;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=3-ketosteroid-9-alpha-hydroxylase reductase subunit {ECO:0000313|EMBL:SQG47922.1};
DE EC=1.17.1.- {ECO:0000313|EMBL:SQG47922.1};
DE SubName: Full=Phenylacetate-CoA oxygenase/reductase, PaaK subunit {ECO:0000313|EMBL:ACS31493.1};
GN Name=hmp_1 {ECO:0000313|EMBL:SQG47922.1};
GN OrderedLocusNames=Mlut_20190 {ECO:0000313|EMBL:ACS31493.1};
GN ORFNames=NCTC2665_00692 {ECO:0000313|EMBL:SQG47922.1};
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS31493.1, ECO:0000313|Proteomes:UP000000738};
RN [1] {ECO:0000313|EMBL:ACS31493.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS31493.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT "Complete sequence of Micrococcus luteus NCTC 2665.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX PubMed=19948807; DOI=10.1128/JB.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [3] {ECO:0000313|EMBL:SQG47922.1, ECO:0000313|Proteomes:UP000248985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG47922.1,
RC ECO:0000313|Proteomes:UP000248985};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; CP001628; ACS31493.1; -; Genomic_DNA.
DR EMBL; LS483396; SQG47922.1; -; Genomic_DNA.
DR RefSeq; WP_010080098.1; NZ_WBMF01000019.1.
DR AlphaFoldDB; C5C705; -.
DR STRING; 465515.Mlut_20190; -.
DR EnsemblBacteria; ACS31493; ACS31493; Mlut_20190.
DR KEGG; mlu:Mlut_20190; -.
DR PATRIC; fig|465515.4.peg.1954; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_1_11; -.
DR Proteomes; UP000000738; Chromosome.
DR Proteomes; UP000248985; Chromosome 1.
DR GO; GO:0051537; F:2 iron, 2 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 GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011884; PaaE.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR02160; PA_CoA_Oxy5; 1.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:SQG47922.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000738}.
FT DOMAIN 15..119
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 298..389
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 389 AA; 42769 MW; 8E47FAD0D280111D CRC64;
MTETTDAPTT GKRRATFNTL EVSELRRLTD DSVEVTFAVP EELADDYDYV PGQYVALRKE
LDGAEVRRSY SICAVPKRGE IRVAVKKDIG GRFSTWANES LEVGEKIDVM NPQGAFTSRT
HVTSLNDAQK VAAEKVAEKK DTHLVAFAAG SGITPIMAIA KAVLAASETS RFDLVYANRS
AMDVMFAEEI GDLKDKYPAR FTVHHVLSRE QRVSPLLSGR IDEDKLTTLL DRVIDVEGTD
EWFLCGPFEL VQLTRETLAA RGVSEDDVRF ELFTTGRPEN PQGHSGRVVE VDPKGDNVTI
EFNLDGLTAK VESPKSAHET VLNAALRVRS DVPFACAGGV CGTCRAKVVD GAYEMDENYA
LEKDEVEKGY VLTCQTRPTS DSITLDFDA
//
