ID A0A3R9MNT2_9BACI Unreviewed; 637 AA.
AC A0A3R9MNT2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|HAMAP-Rule:MF_01107};
DE Includes:
DE RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
DE Includes:
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=argD {ECO:0000256|HAMAP-Rule:MF_01107};
GN Synonyms=argB {ECO:0000256|HAMAP-Rule:MF_00082};
GN ORFNames=EJF36_06030 {ECO:0000313|EMBL:RSK26451.1};
OS Bacillus sp. HMF5848.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK26451.1, ECO:0000313|Proteomes:UP000274811};
RN [1] {ECO:0000313|EMBL:RSK26451.1, ECO:0000313|Proteomes:UP000274811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF5848 {ECO:0000313|EMBL:RSK26451.1,
RC ECO:0000313|Proteomes:UP000274811};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000256|HAMAP-Rule:MF_00082}.
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:0000256|HAMAP-
CC Rule:MF_01107};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00082};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01107};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01107};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_00082}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC 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_00082}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00082}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01107}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSK26451.1}.
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DR EMBL; RWIV01000001; RSK26451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9MNT2; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000274811; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04238; AAK_NAGK-like; 1.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-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 HAMAP; MF_00082; ArgB; 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00761; argB; 1.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00082};
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW ECO:0000313|EMBL:RSK26451.1};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00082};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01107}; Reference proteome {ECO:0000313|Proteomes:UP000274811};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000313|EMBL:RSK26451.1}.
FT DOMAIN 11..235
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 48..49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 349..350
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 376
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 379
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 461..464
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 519
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT BINDING 520
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT SITE 15
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 217
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT MOD_RES 491
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ SEQUENCE 637 AA; 69193 MW; 3CF36C956D0F0DCE CRC64;
MREGDLLMQD IVVVKCGGSI LRELSHHFFD SLLALQANGY QVVLVHGGGP DISAKLAAHH
IPSTFVDGLR YTSNQAMQIV NDMLLQLNEQ FVRKLNAENV AACGVGTVLQ AAFKNKEKYG
YVGEATATDV NAIRIILNDK HIPVIVPLGM TENGELLNIN ADSAAGAIAR DLQARHLLFV
TDVPGILVNR NVLKEATKDH IEQLIENGTI YGGMIPKVKS ALTCLEHGAN QVMIVAENFY
EGNTVKGTKI VEKKTSHLFP TYARWSLHIE YGEGSYLYSK DGKKYLDFVS GIAVCNLGHR
HHAVESAVSE QMQKYWHLSN LFPISLQEEV AEILTSHSDT DLAFFCNSGA EANEAAIKLA
RKYTKRHKII TFEKSFHGRT FATMSATGQA KIHDGYGPLL PEFVYLPLND SDALEATMNT
EVAAVMVEIV QGEGGVVVAQ DEFLQKLAAL CQQNGTLLIV DEVQTGIGRT GTAFAYQHVP
HLSPDIITSA KGIANGLPLG VMLGKMNLAE AFGPGSHGST FGGNPLSLAA AKASLEIIFN
DAFLQTVSEK GCYLRDELKK HVYTIPFVKD IRGKGLMIGI ACEVDVSSVI VELQQQGLLA
LTAGPNVIRL LPPLTISQQE MDEAVTIITD VLNNYCV
//
