(data stored in SCRATCH zone)

SWISSPROT: C6WDX2_ACTMD

ID   C6WDX2_ACTMD            Unreviewed;       355 AA.
AC   C6WDX2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Putative phenylalanine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01513};
DE            EC=2.6.1.- {ECO:0000256|HAMAP-Rule:MF_01513};
GN   Name=pat {ECO:0000256|HAMAP-Rule:MF_01513};
GN   OrderedLocusNames=Amir_0146 {ECO:0000313|EMBL:ACU34117.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34117.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34117.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01513}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01513,
CC         ECO:0000256|SAAS:SAAS00655984};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|HAMAP-Rule:MF_01513}.
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DR   EMBL; CP001630; ACU34117.1; -; Genomic_DNA.
DR   RefSeq; WP_012782780.1; NC_013093.1.
DR   ProteinModelPortal; C6WDX2; -.
DR   STRING; 446462.Amir_0146; -.
DR   EnsemblBacteria; ACU34117; ACU34117; Amir_0146.
DR   KEGG; ami:Amir_0146; -.
DR   eggNOG; ENOG4105CIH; Bacteria.
DR   eggNOG; COG0079; LUCA.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; HGFLVYR; -.
DR   OrthoDB; POG091H05S1; -.
DR   Proteomes; UP000002213; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WDX2.
DR   SWISS-2DPAGE; C6WDX2.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00766461, ECO:0000313|EMBL:ACU34117.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00655949};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00766408, ECO:0000313|EMBL:ACU34117.1}.
FT   DOMAIN       25    346       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   MOD_RES     221    221       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01513}.
SQ   SEQUENCE   355 AA;  38152 MW;  5D66C5D0717ED293 CRC64;
     MSVRTRPDLS LLPPYVPGRS VPGAIKLASN EVSAGPLPSV VRAIADAATS VNRYPDSGSG
     ALVERLSGKL GVPEEQIAVG CGSVTLCQQL VQATCGEGDE VLFPWRSFEA YPIITQVVGA
     TQRRVPLTPE HGLDLDAMAE AITPSTRLVF VCNPNNPTGT AVRTEEVERF VERVPDDVLV
     VLDEAYKEFV DDPHVPDGVE LAKAHWSRGR DNVAVLRTFS KAYGLAGLRV GYAVGSPQVA
     DALRKVYVPF GVNALAQVAA IASLDAEPEL LERCRGLVVE RGRVRAELLA AGYEVPETQA
     NFVWLPLGER TAAFNEHCLD RKVVVRAFAG DGARVTIGSP EENEAFLVAA RSFER
//

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