ID A0A0A2JTZ2_PENEN Unreviewed; 1046 AA.
AC A0A0A2JTZ2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II {ECO:0000313|EMBL:KGO58894.1};
GN ORFNames=PEX2_092490 {ECO:0000313|EMBL:KGO58894.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO58894.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO58894.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO58894.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO58894.1}.
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DR EMBL; JQFZ01000110; KGO58894.1; -; Genomic_DNA.
DR RefSeq; XP_016600235.1; XM_016746519.1.
DR AlphaFoldDB; A0A0A2JTZ2; -.
DR STRING; 27334.A0A0A2JTZ2; -.
DR GeneID; 27681939; -.
DR HOGENOM; CLU_003662_1_0_1; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01558; POR; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KGO58894.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 659..897
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1046 AA; 114621 MW; EEDEF9BC6730D535 CRC64;
MGSSVPALSA LNGPTYVTAQ TLIQQVAYLL SDKIFSYSPE TFDLDAALKE WTSKGETNAN
GESPSVKALE TRQGAGNMAL GYLFSQDFDL KKRHIPQGIV ASSATLPYMR AALEQLSLLY
SVASPVAAHV AAVDYAGEDG LVSDYASALS LAEDLGLGLV SSGSAHESQH MALFTTLLSS
VLPSIHIYDG VRVGRDTTRI IDVLDKDGLT RTYETVRKSL DESRNRHLDA QGKVLDLLKT
LNGELGTDYG AFEYHGHSEP TSVLIAFGTV EAALTAQIAR SLAKDGVRVG VVNVRVYRPF
IEEEFLRVLP QSTKTVAVLG QVASEQAVQE EGIHSALYED VLASLTFATG REHNPGCVEI
KYPRSQRWDL ISTAAAFQRV YDQPILTVDG ETNASLQLLD PASVQEYTFW DVDTSVTEAA
AQTLSQALGA DSASNVTLSQ THDNLVQGGA IRVDIRKSAK IVDAPYAVTA AEVSYVGNIS
LLNDVDVLAS VKDNAKVIVN APGVKDEDLE KKLPATFKQA VAQRGISVFV VDSSAIEDSS
LSALVLQASF VRVALPAQEA LATKKLSSIT GNAEALDNVT KDLEKVLRQI EVPESWKEPE
GVSEAVQLPK DIIVNSFVSF DKNESEPPTL LKDWETAARG LAFKEAYGTR DALRPDLAHK
TFTVHVKENR RLTPPTYDRN IFHIEFDIGE TGLKYDIGEA LGIHAENDPE DIKKFIEFYG
LDADAIVEVP SREDPAVLEN RTVYQALVQN VDIFGRPPKR FYEALAEFAS DEKEKANLLI
LGGPDGATEF KRRAEVDTVT FADILLEYPS AHPDFHEIVR IIGPLKRREY SIASCQKVTP
TSVALMIVAV NWVDPNGRDR FGLATRFLSR LQVGSPITVS VKSSVMKLPP KSTQPLIMAG
LGTGLAPFRA FVQHRALEKA QGKEIGAVLL YMGSRHQREE YCYGEEWEAY QEAGVITLLG
AAFSRDQPEK IYIQDRMRQT LPEIIQAYIR EEGAFYLCGP TWPVPDVTAV LEEAIATEAK
NNGKKVDTRK EIEKLKDEER YVLEVY
//
