ID   ARLY_VIBVY              Reviewed;         624 AA.
AC   Q7MH73;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Bifunctional protein ArgH;
DE   Includes:
DE     RecName: Full=Argininosuccinate lyase;
DE              Short=ASAL;
DE              EC=4.3.2.1;
DE     AltName: Full=Arginosuccinase;
DE   Includes:
DE     RecName: Full=Probable acetyltransferase;
DE              EC=2.3.1.-;
GN   Name=argH; OrderedLocusNames=VV2999;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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   -!- 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   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000305}.
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DR   EMBL; BA000037; BAC95763.1; -; Genomic_DNA.
DR   RefSeq; WP_011079348.1; NC_005139.1.
DR   AlphaFoldDB; Q7MH73; -.
DR   SMR; Q7MH73; -.
DR   STRING; 672.VV93_v1c27270; -.
DR   PRIDE; Q7MH73; -.
DR   EnsemblBacteria; BAC95763; BAC95763; BAC95763.
DR   KEGG; vvy:VV2999; -.
DR   eggNOG; COG0165; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
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; Reference proteome; Transferase.
FT   CHAIN           1..624
FT                   /note="Bifunctional protein ArgH"
FT                   /id="PRO_0000137849"
FT   DOMAIN          464..614
FT                   /note="N-acetyltransferase"
FT   REGION          1..466
FT                   /note="Argininosuccinate lyase"
FT   REGION          467..624
FT                   /note="Probable acetyltransferase"
SQ   SEQUENCE   624 AA;  69430 MW;  3DCAAC6A7D2EEE7F CRC64;
     MALWGGRFTQ AADTRFKDFN DSLRFDYRLA EQDIVGSIAW SKALLSVNVL SKEEQQKLEF
     ALNELKLEVM EDPHQILHSD AEDIHSWVEQ QLIGKVGDLG KKLHTGRSRN DQVATDLKLW
     CRQQGHQLLL GLDKLQTQMV NVAKQHQATV LPGYTHLQRA QPVTFAHWCL AYVEMFERDY
     SRLSDALTRL DTCPLGSGAL AGTAYPIDRE QLAQDLGFRR ATRNSLDSVS DRDHVMELMS
     VASISMLHLS RLAEDMIFYN SGESGFIELA DTVTSGSSLM PQKKNPDALE LIRGKTGRVY
     GSLAGMMMTV KALPLAYNKD MQEDKEGLFD ALDTWNDCME MAALCFDGIK VNGERTLEAA
     KQGYANSTEL ADYLVAKGIP FREAHHIVGV AVVGAIAQGC ALEELSLEQL QSFSPVIEAD
     VYQILTIESC LEKRSALGGV SPKQVAYAVE QADKRLAARD TTLVKVRPAR ITDIETLESM
     VAYWANLGEN LPRTRSEIIR DIGLFAVSEH QGLVTGCASL YIYDSGLAEI RSLGIEAGWQ
     RQGQGTAVVQ YLIDKAKDMA IKKLFVLTRA PEFFLKQNFV QTSKSLLPEK VLKDCDQCPR
     QHACDEVALE FNLSEQIISQ VKVA