ID Q7V678_PROMM Unreviewed; 502 AA.
AC Q7V678;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Putative glycolate oxidase subunit glcD {ECO:0000313|EMBL:CAE21470.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:CAE21470.1};
GN Name=glcD {ECO:0000313|EMBL:CAE21470.1};
GN OrderedLocusNames=PMT_1295 {ECO:0000313|EMBL:CAE21470.1};
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE21470.1, ECO:0000313|Proteomes:UP000001423};
RN [1] {ECO:0000313|EMBL:CAE21470.1, ECO:0000313|Proteomes:UP000001423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; BX548175; CAE21470.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7V678; -.
DR DNASU; 1727793; -.
DR KEGG; pmt:PMT_1295; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_3; -.
DR Proteomes; UP000001423; Chromosome.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
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 InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 Oxidoreductase {ECO:0000313|EMBL:CAE21470.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001423}.
FT DOMAIN 51..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 502 AA; 53973 MW; 3C04C390738AA258 CRC64;
MLPRLLDRCA GMVSHDWTAL DRDLRRFLPK KSVVSKRQEL LVYDCDGLTI DRHCPPLAVL
PETTEEVSQI LACCHRHSIP FVARGSGTGL SGGALVEQEA LLVVTSRMRR ILSMDLDNHT
ITVQPGVINS WVTRAVAGEG FYYAPDPSSQ VVCSIGGNVA ENSGGVHCLK YGVTSNHVLG
LEVVLADGTV TLLGGGLPEH AELDLRGAFI GSEGTLGIAT AITLRLLRAP QHVTVLLADF
PTMESAGEAV CQVTAAGVLP AGMEIMDNFM INAVNDLFGF DEYPRDAAAV LLIELDGQAA
EVTVAADQAS GLCSKAGART IRRAEEPADR ALLWKGRKSA FAAVGQISPT YYVQDGVVPR
STLPRVLMAI ERLSREYELP VANVFHAGDG NLHPLILYNA DTPDVESRVR DLGSAILREC
LDVGGSITGE HGVGADKRCY LDWMFAADDL STMKLLRRAF DPDGRANPDK IFPTPKSCGE
SARRQVILTS EGLEMPSEAK AF
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