(data stored in ACNUC7421 zone)

SWISSPROT: Q3IFT9_PSEHT

ID   Q3IFT9_PSEHT            Unreviewed;       401 AA.
AC   Q3IFT9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 98.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
GN   Name=astC {ECO:0000313|EMBL:CAI85297.1};
GN   Synonyms=argD {ECO:0000256|HAMAP-Rule:MF_01107};
GN   OrderedLocusNames=PSHAa0194 {ECO:0000313|EMBL:CAI85297.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85297.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85297.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC       acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate
CC       aminotransferase activity, thus carrying out the corresponding
CC       step in lysine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
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DR   EMBL; CR954246; CAI85297.1; -; Genomic_DNA.
DR   RefSeq; WP_011326912.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFT9; -.
DR   STRING; 326442.PSHAa0194; -.
DR   EnsemblBacteria; CAI85297; CAI85297; PSHAa0194.
DR   KEGG; pha:PSHAa0194; -.
DR   PATRIC; fig|326442.8.peg.187; -.
DR   eggNOG; ENOG4105C8Y; Bacteria.
DR   eggNOG; COG4992; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00821; -.
DR   OMA; MDRVLVH; -.
DR   OrthoDB; POG091H03ZS; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR017652; Ac/SucOrn_transaminase_bac.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR11986:SF101; PTHR11986:SF101; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03246; arg_catab_astC; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFT9.
DR   SWISS-2DPAGE; Q3IFT9.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768889, ECO:0000313|EMBL:CAI85297.1};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00768842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768841, ECO:0000313|EMBL:CAI85297.1}.
FT   REGION      103    104       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   REGION      221    224       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     136    136       Pyridoxal phosphate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     139    139       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     278    278       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     279    279       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01107}.
FT   MOD_RES     250    250       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
SQ   SEQUENCE   401 AA;  42768 MW;  908CB1F47BB6FE9E CRC64;
     MTVNRELFDH VMVPNYAPSS VIPVRGEGSR VWDQQGREFI DFAGGIAVNC LGHCHPALVG
     ALKEQGEKLW HLSNVMTNEP ALRLAKKMVD ATFAEKVYFA NSGAEANEAA LKLARRFALD
     QFGAEKSQII AFNKGFHGRT FFTVTVGGQA AYSDGFGPKP GDIVHCDYND LAAFEALISD
     KTCAVMMEPL QGEGGIVSPT DEFAQGVRDL CTKHNALLIF DEVQTGVGRT GNLYAYQGLN
     VVPDILTTAK ALGGGFPIGA MITTTEIAQH LKVGTHGSTY GGNPLACAVA EAAFDTVNTP
     EVLAGVTAKA ALFNQLLTEI NNKYHVFSEI RGQGLLIGAV VSEQYKGRAK EFLVAGTEHG
     LMSLVAGADV VRFTPSLVIP EADIREGMAR FEKAVASVVS A
//

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