ID   ARGHA_MORAB             Reviewed;         629 AA.
AC   Q9K3D6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Bifunctional protein ArgHA;
DE   Includes:
DE     RecName: Full=Argininosuccinate lyase;
DE              Short=ASAL;
DE              Short=Arginosuccinase;
DE              EC=4.3.2.1;
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase;
DE              EC=2.3.1.1;
DE     AltName: Full=N-acetylglutamate synthase;
DE              Short=AGS;
DE              Short=NAGS;
GN   Name=argHA;
OS   Moritella abyssi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=111292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2693;
RX   PubMed=10692366; DOI=10.1128/jb.182.6.1609-1615.2000;
RA   Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.;
RT   "Evolution of arginine biosynthesis in the bacterial domain: novel gene-
RT   enzyme relationships from psychrophilic Moritella strains (Vibrionaceae)
RT   and evolutionary significance of N-alpha-acetyl ornithinase.";
RL   J. Bacteriol. 182:1609-1615(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC         Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:57472; EC=4.3.2.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC       ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC       fulfills an anaplerotic role.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the acetyltransferase
CC       family. ArgA subfamily. {ECO:0000305}.
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DR   EMBL; AJ252021; CAB95024.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9K3D6; -.
DR   SMR; Q9K3D6; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR011244; ASAL_AGS_AcTrfase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43814; PTHR43814; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PIRSF; PIRSF036456; ASAL_AGS; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Lyase; Multifunctional enzyme; Transferase.
FT   CHAIN           1..629
FT                   /note="Bifunctional protein ArgHA"
FT                   /id="PRO_0000186813"
FT   DOMAIN          464..598
FT                   /note="N-acetyltransferase"
FT   REGION          1..499
FT                   /note="Argininosuccinate lyase"
FT   REGION          500..629
FT                   /note="Amino-acid acetyltransferase"
SQ   SEQUENCE   629 AA;  69497 MW;  A9EF306A299539BF CRC64;
     MALWGGRFSQ AADARFKSFN DSLRFDYRLA EQDITGSVAW SKALVSVGIL TQDEQLTIEA
     ALNDLKLAVL ENPEQILQSD AEDIHSWVET QLIAKVGDLG KKLHTGRSRN DQVATDLKLW
     CKQQGQQLLM QLDKTQQQLV SLAREHQHTV LPGYTHLQRA QPVTFSHWCL AYVEMLERDF
     SRLTDCLKRL DTCPLGSGAL AGTAYPMDRT ELAHSLGFGS ATLNSLDSVS DRDHVMELMC
     TASMSMIHLS RLAEDLIFYN SGESNFIELA DAVTSGSSLM PQKKNPDALE LIRGKTGRVF
     GSLSAMLMTL KALPLAYNKD MQEDKEGLFD ALDTWSDCLE MAAMSLVGMK INEARTKEAA
     LGGYSNATEL ADYLVAKGVP FRDSHHIVGE AVVAAIAKGV PLEALTLAEF KAFDVLIEDD
     VYHHLSLDET LAKRKALGGV SPVQVEFALT NAEKRLEERD TSGISIRAAR LTDLDDIERM
     VNYWANIGEN LPRSRSDLVK AVGTFAVTEK HNQVTGCASI YVYDTGLAEL RSLGIEPGYQ
     GGGQGKAVVE YMLRKAEQMA IQKVFVLTRV PEFFMKLGFR STSKSMLPEK VLKDCDMCPR
     QHACDEVALE FKLNVVGQTI NLKAEKLAS