ID F0UA03_AJEC8 Unreviewed; 925 AA.
AC F0UA03;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phosphatidate cytidylyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00018337};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487};
DE AltName: Full=CDP-diacylglycerol synthase {ECO:0000256|ARBA:ARBA00029893};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|ARBA:ARBA00030262};
GN ORFNames=HCEG_02831 {ECO:0000313|EMBL:EGC43616.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443}.
CC -!- SIMILARITY: Belongs to the TAM41 family.
CC {ECO:0000256|ARBA:ARBA00005458}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR EMBL; DS990637; EGC43616.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UA03; -.
DR STRING; 544711.F0UA03; -.
DR VEuPathDB; FungiDB:I7I53_10225; -.
DR VEuPathDB; FungiDB:I7I53_10226; -.
DR HOGENOM; CLU_315672_0_0_1; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR015222; Tam41.
DR NCBIfam; TIGR01141; hisC; 1.
DR PANTHER; PTHR13619:SF0; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13619; UNCHARACTERIZED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF09139; Tam41_Mmp37; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EGC43616.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGC43616.1}.
FT DOMAIN 579..911
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 38..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 102834 MW; 8D50723B58F383EF CRC64;
MAVSHLPFLL IRPRLTAPSR LHIFIPPLSS DQYSHKCYRP LSTESSPSPH DRDSGPLPGF
NAAAHKDLNS PSNVSPASSN SGQSIPLSES GTNWYDNPDF TISTFSELPS KNFGVNQHMI
INEEFKEALR QILWQFKAPI RYAFAYGSGV FPQSNRSATP AESSHPAAPQ AIQTGQGNSG
KMIDFIFGVS YSQHWHALNL NQHRDHYSGL GSLGSYVVSQ IQEKWGAGVY FNPYVTVNGT
LIKYGVVNID TLCKDLSDWD SLYLAGRLQK PVKILRDHPK VRLANQVNLL SAVRVALLLL
PPKFTEQQLY STIAGISYLG DPRMSFASED PRKVNNIVTS QMTNFRRLYA PLIETLPNVA
FNDPQCARLD WVDNPEVDAW LAQDMDPFKR GNMVRRLPQS FREKLYFQFQ SRYQIPRVEF
EKMVEKSNDE DPERVHRRVG GVFEQRIAAD EHLKDEATKS IRKTISWPST NQSIKSLFTA
GLGRGWRYMK EKQQKYASAK QETEGPRISR LTSQNVQGLI SFNCGHIVAQ ENDGTNVLLD
ANENAYGPGL VLNSEGRIQK GLSAATATAS ENSSFPDIDF LGLNRYPDPH QIELKQLLCN
LRNTHVHTQN TLTPDRLFVG VGSDEVIDAL LRCFCTPGHD QILTCPPTYG MYSVSAQIND
ISIVKVPLDT SNNFRLRPEA INEVLSSTPS IKLVYICSPG NPTANLIRKD DIQKVLEHPT
WNGVVVVDEA YIDFAPEGSS LAEWVAEWPN LVVMQTLSKA FGLAGIRLGA AFTSPEIARL
LNSLKAPYNI SSPTSALAKA VLATENVALM NRNKKKILVQ RDRLISELPK VPGIGRFLGG
MDSNFLLVEV LDRPAEEGGK PCNDMALAVY KALAEKKGVV VRFRGNEDGC KGCLRITVGT
ETEVSKFLRE IQVVLSDIYA TKGLK
//
