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PATR_MYCTU
ID   PATR_MYCTU              Reviewed;         353 AA.
AC   P9WML5; L0TGI3; P72039;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Putative phenylalanine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01513};
DE            EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_01513};
GN   Name=pat {ECO:0000255|HAMAP-Rule:MF_01513}; Synonyms=hisC2;
GN   OrderedLocusNames=Rv3772; ORFNames=MTCY13D12.06;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: May catalyze the transamination reaction in phenylalanine
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01513}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01513};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255|HAMAP-Rule:MF_01513}.
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DR   EMBL; AL123456; CCP46601.1; -; Genomic_DNA.
DR   PIR; H70694; H70694.
DR   RefSeq; NP_218289.1; NC_000962.3.
DR   RefSeq; WP_003899686.1; NZ_NVQJ01000009.1.
DR   PDB; 4R2N; X-ray; 1.98 A; A/B/C/D=2-353.
DR   PDB; 4R5Z; X-ray; 1.95 A; A/B/C/D=2-353.
DR   PDBsum; 4R2N; -.
DR   PDBsum; 4R5Z; -.
DR   AlphaFoldDB; P9WML5; -.
DR   SMR; P9WML5; -.
DR   STRING; 83332.Rv3772; -.
DR   PaxDb; P9WML5; -.
DR   DNASU; 886105; -.
DR   GeneID; 886105; -.
DR   KEGG; mtu:Rv3772; -.
DR   TubercuList; Rv3772; -.
DR   eggNOG; COG0079; Bacteria.
DR   OMA; YPDMACT; -.
DR   PhylomeDB; P9WML5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   HAMAP; MF_01513; Phe_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR024892; Pat.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..353
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153517"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           60..70
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           113..119
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           136..141
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           165..174
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           199..205
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          209..217
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           233..242
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           250..261
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           263..287
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           307..316
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:4R5Z"
FT   HELIX           336..352
FT                   /evidence="ECO:0007829|PDB:4R5Z"
SQ   SEQUENCE   353 AA;  38040 MW;  E5E49F74DC2436F4 CRC64;
     MTARLRPELA GLPVYVPGKT VPGAIKLASN ETVFGPLPSV RAAIDRATDT VNRYPDNGCV
     QLKAALARHL GPDFAPEHVA VGCGSVSLCQ QLVQVTASVG DEVVFGWRSF ELYPPQVRVA
     GAIPIQVPLT DHTFDLYAML ATVTDRTRLI FVCNPNNPTS TVVGPDALAR FVEAVPAHIL
     IAIDEAYVEY IRDGMRPDSL GLVRAHNNVV VLRTFSKAYG LAGLRIGYAI GHPDVITALD
     KVYVPFTVSS IGQAAAIASL DAADELLART DTVVAERARV SAELRAAGFT LPPSQANFVW
     LPLGSRTQDF VEQAADARIV VRPYGTDGVR VTVAAPEEND AFLRFARRWR SDQ
 
 
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