ID A0A0A2IFK0_PENEN Unreviewed; 765 AA.
AC A0A0A2IFK0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Histidine phosphatase superfamily, clade-2 {ECO:0000313|EMBL:KGO51161.1};
GN ORFNames=PEX2_106860 {ECO:0000313|EMBL:KGO51161.1};
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:KGO51161.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO51161.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO51161.1,
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 -!- 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:KGO51161.1}.
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DR EMBL; JQFZ01000308; KGO51161.1; -; Genomic_DNA.
DR RefSeq; XP_016594165.1; XM_016747954.1.
DR AlphaFoldDB; A0A0A2IFK0; -.
DR STRING; 27334.A0A0A2IFK0; -.
DR GeneID; 27683375; -.
DR HOGENOM; CLU_020880_2_0_1; -.
DR OrthoDB; 2721627at2759; -.
DR PhylomeDB; A0A0A2IFK0; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR20963:SF43; PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01240)-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 2..193
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 765 AA; 84380 MW; CA912098AEF23E1E CRC64;
MTTSSAAASR FKPGDWMTLL SEGMHATKLR IDLCLAVHIP DSMSFEEAAA LPMVHPTVYH
ALVNVAKLRP GQSVVVQAAV ASRISALLME KYNVLEAHIF HSCDTSFCKP IKRIMVGHDL
DCVLNSSEDS LVVTHPTTNS PACGLSTAER TGSPVFHTLW SENERRNRVT ILREDRTGQG
GEITWTLQGG TTIPRKSIGE FITVNKSKVQ SYLIYCTYLP QREVEVNRGA IPLQETQGFQ
STMKNFIGAT LVTAAVTATA SRTSAPAPGP TGSSYASGFD MTASWANLSP YKDADSFGLP
SGVPQGCELS QVHVLHRHAQ RFPTDYPLDG EGMTDFAAKL TNYSKAHPNK TVALGPLKFL
NNWDYVIGQD ILMENGAATE ATSGANFWIK YGRLLYRAGR ENAAAWSSSL NVYANGTDRP
TPVFRTTSQA RILESARWWL SGFFGNSGAN SSYDQYNLVV IPEQADFNNT LASYETCTFD
YSEGDNAAEV FISRYTKHAR TRLSAYFPRD FNLTSMDVLA MQNLCVYEST SLGGSSFCSL
FTEQEWKDFE YNVDVQYYGD YAYGSPSGRA QGIGYVLELA ARLEEKLINS SDTSINYTYT
NNEAQFPFGQ PFYMDMSHDD IILSVINALG FDYFKYGPKG LPVHIDHAPE RNFSLSQMTP
FGARFISEIW TCPRDVSFDD LDPVLYANPT IMSTTNTTKY IRFVLNNSPV PQDGLIGCED
SSNGFCHLDK FLSGIPTLKD KAQFQKACFG NYTTGSQVGD GAPES
//
