ID A0A135LSS1_PENPA Unreviewed; 598 AA.
AC A0A135LSS1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Citrate synthase-like, core {ECO:0000313|EMBL:KXG51976.1};
GN ORFNames=PGRI_082600 {ECO:0000313|EMBL:KXG51976.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG51976.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG51976.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG51976.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000256|ARBA:ARBA00005495}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566}.
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:KXG51976.1}.
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DR EMBL; LHQR01000027; KXG51976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LSS1; -.
DR STRING; 5078.A0A135LSS1; -.
DR OMA; WVAHWNE; -.
DR OrthoDB; 642531at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF04828; GFA; 1.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 3..116
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000259|PROSITE:PS51891"
SQ SEQUENCE 598 AA; 66567 MW; 8DA3FD50AA448F10 CRC64;
MPLSGHCLCK AVTYTVDVDA PLVTGYDHCD DCQRQSGSTY SLVAVVPKDK LTIQGPTKSW
AGKGSSGLAV HRIFCSECGS PIAHDPDAAP EIIAIKAGTL DTEIKKNLKP DTEIWTVGKL
PFCQENLARP FKHMPDNRRI FVGKVIQPIL WVCHMCFTMS GTLFIHDSRT YVNYEIPINQ
NSVRAIDLQR IRAPSLNSNH ADQLAHGLRV YDPGLQNTAV TQSAISFSDH ENSLLLYRGY
TLDQLWGCDF EEMFHLLLWG KYPTASQSEE LRQRLAQYMQ EVPDIVRQTI FNLPKTTSPL
PLIIAGLSAY LACILDVIPA TTNATVFQTD FKRADQVILQ TAAAYAVVFG AVRSHRIGIP
WRSPSPHQTY YENLFTMAGL VDPETNRPDP IRVSCFRRFG NLNAEHGMAL SVFSALVTAS
SLTDPVSCLI SAVAAAHGPL HFGATESAQR ALHDIGELEN VPAFIEEIKA GKRKLFGYGH
RTYKGMDPRV RPIQSILKDL AYVHQPLLKV AEAIEETAAK DDYFSARGLY PNADFYGQFV
FTGIGFEPDI IPAAMLAHRI MGIMAHWREY MVTRGKLFRP THLYTGYTEL NPDPRAKI
//
