ARLY_NEIG1
ID ARLY_NEIG1 Reviewed; 458 AA.
AC Q5FA15;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=NGO0219;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; AE004969; AAW88972.1; -; Genomic_DNA.
DR RefSeq; WP_003704829.1; NC_002946.2.
DR RefSeq; YP_207384.1; NC_002946.2.
DR AlphaFoldDB; Q5FA15; -.
DR SMR; Q5FA15; -.
DR STRING; 242231.NGO_0219; -.
DR EnsemblBacteria; AAW88972; AAW88972; NGO_0219.
DR KEGG; ngo:NGO_0219; -.
DR PATRIC; fig|242231.10.peg.271; -.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
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; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
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; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..458
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240741"
SQ SEQUENCE 458 AA; 51310 MW; 705B0FF8F6B50540 CRC64;
MHDKTWSGRF NEPVSELVKQ YTASIGFDQR LAEWDIQGSL AHAQMLTRSG VLSENDLTDI
RRGMSEILEE IRSGKIEWPL DLEDVHMNIE RRLTDKIGDA GKRLHTGRSR NDQVATDIRL
WLRDQITVIQ NLIQNLQTAL LDLAEQNAEA VMPGFTHLQV AQPVSFGHHM LAYVEMLGRD
FERMTDCRKR VNRMPLGAAA LAGTTYPIQR EITAELLGFE QICQNSLDAV SDRDFAIEFT
AAASLVMVHL SRLSEELILW MSPRFGFIDI ADRFCTGSSI MPQKKNPDVP ELVRGKSGRV
IGHLIGLITL MKSQPLAYNK DNQEDKEPLF DTADTLIDTL RIYADMMRGV TVKPGNMRAA
VMQGFATATD LADYLVKKGM PFRDAHEVVA QAVRHADEAG VDLSELPLEA LQGFSKLISD
DVYGVLTPEG SLNARNHLGG TAPEQVRLQV KRWREMSA