ARGD_MYCTU
ID ARGD_MYCTU Reviewed; 400 AA.
AC P9WPZ7; L0T8W6; P63568; P94990;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107};
DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107};
GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; OrderedLocusNames=Rv1655;
GN ORFNames=MTCY06H11.20;
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, DETERMINATION OF TRANSLATIONAL START
RP SITE, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT THR-2.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17259624; DOI=10.1099/mic.0.2006/001537-0;
RA Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.;
RT "Experimental determination of translational starts using peptide mass
RT mapping and tandem mass spectrometry within the proteome of Mycobacterium
RT tuberculosis.";
RL Microbiology 153:521-528(2007).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP PUPYLATION AT LYS-314, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01107};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01107};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP-
CC Rule:MF_01107}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01107}.
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DR EMBL; AL123456; CCP44420.1; -; Genomic_DNA.
DR PIR; B70621; B70621.
DR RefSeq; NP_216171.1; NC_000962.3.
DR RefSeq; WP_003408163.1; NZ_NVQJ01000069.1.
DR PDB; 7NN1; X-ray; 1.54 A; A/B/C/D=1-400.
DR PDB; 7NN4; X-ray; 1.47 A; A/B/C/D=1-400.
DR PDB; 7NNC; X-ray; 1.70 A; A/B/C/D=1-400.
DR PDBsum; 7NN1; -.
DR PDBsum; 7NN4; -.
DR PDBsum; 7NNC; -.
DR AlphaFoldDB; P9WPZ7; -.
DR SMR; P9WPZ7; -.
DR STRING; 83332.Rv1655; -.
DR iPTMnet; P9WPZ7; -.
DR PaxDb; P9WPZ7; -.
DR PRIDE; P9WPZ7; -.
DR DNASU; 885187; -.
DR GeneID; 885187; -.
DR KEGG; mtu:Rv1655; -.
DR TubercuList; Rv1655; -.
DR eggNOG; COG4992; Bacteria.
DR OMA; PFMVPTY; -.
DR PhylomeDB; P9WPZ7; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00707; argD; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Arginine biosynthesis; Cytoplasm; Isopeptide bond; Pyridoxal phosphate;
KW Reference proteome; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17259624,
FT ECO:0007744|PubMed:21969609"
FT CHAIN 2..400
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112756"
FT BINDING 113..114
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 139
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 142
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 224..227
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 281
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT MOD_RES 2
FT /note="N-acetylthreonine; partial"
FT /evidence="ECO:0000269|PubMed:17259624,
FT ECO:0007744|PubMed:21969609"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT CROSSLNK 314
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:7NN4"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7NN4"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:7NN4"
FT TURN 226..233
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:7NN4"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:7NN4"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 287..302
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:7NN4"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:7NN4"
FT HELIX 379..396
FT /evidence="ECO:0007829|PDB:7NN4"
SQ SEQUENCE 400 AA; 40910 MW; 833846D529795019 CRC64;
MTGASTTTAT MRQRWQAVMM NNYGTPPIAL ASGDGAVVTD VDGRTYIDLL GGIAVNVLGH
RHPAVIEAVT RQMSTLGHTS NLYATEPGIA LAEELVALLG ADQRTRVFFC NSGAEANEAA
FKLSRLTGRT KLVAAHDAFH GRTMGSLALT GQPAKQTPFA PLPGDVTHVG YGDVDALAAA
VDDHTAAVFL EPIMGESGVV VPPAGYLAAA RDITARRGAL LVLDEVQTGM GRTGAFFAHQ
HDGITPDVVT LAKGLGGGLP IGACLAVGPA AELLTPGLHG STFGGNPVCA AAALAVLRVL
ASDGLVRRAE VLGKSLRHGI EALGHPLIDH VRGRGLLLGI ALTAPHAKDA EATARDAGYL
VNAAAPDVIR LAPPLIIAEA QLDGFVAALP AILDRAVGAP
