ID B9M8F8_GEODF Unreviewed; 549 AA.
AC B9M8F8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=p-cresol methylhydroxylase, alpha-prime subunit {ECO:0000313|EMBL:ACM18493.1};
GN Name=pcmI {ECO:0000313|EMBL:ACM18493.1};
GN OrderedLocusNames=Geob_0119 {ECO:0000313|EMBL:ACM18493.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM18493.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM18493.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
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., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM18493.1; -; Genomic_DNA.
DR AlphaFoldDB; B9M8F8; -.
DR STRING; 316067.Geob_0119; -.
DR KEGG; geo:Geob_0119; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_024402_0_1_7; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007721}.
FT DOMAIN 46..239
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 549 AA; 61587 MW; 4B528AB5CA69B7AB CRC64;
MSRFVALPQG VSEATFAKAI QEYRALLGEG RVRTDPASLQ SYMKIMIPES EELHKPSAAM
YPKTVKEIQA IVAIANKYKT PLWTVSTGKN MGYGSSAPAT RGQIVLDLKT MKKIIHVDEE
LGYCLVEPGV TYYDLQQHFK KHKMNLWVDV PAPSAMASPM GNTADRGVGY TPYGEHFLFS
CGMEVVLANG DVIRTGTGGV PNSTSWQANK WGYGPYVDGI FTQSNYGILT KLGVWLMKGP
PPGGYFPFLM KFPKVEMLAD IIKTLMPLRL AQIIPNACIV VNAGWEAAGY FTYDKNGKGT
NRETFYKGKD SLPPKVFQQI MDKYDVGAWN FYAAVYGSPE QVALNWKYVS GAFKAKFGNQ
VRIITEKEAK DDPIFEYRRQ LMMGGSTLQE FGLYNWRGGG GSMWFAPVAA ARPSECDRQM
RLATEVLNKY GFDYVSEFIV GWRDMHHIID LLYDRTDREE MNKAYKCFDE LLTVFTNNGW
GTYRTNTAFM DKVSHSYGPG MRDIHYRLKR ALDPNNILAP GKSGIDLNPH NPGYAFNEGL
NHGRPLDVP
//
