ID B9KF03_CAMLR Unreviewed; 466 AA.
AC B9KF03;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000256|HAMAP-Rule:MF_00006,
GN ECO:0000313|EMBL:ACM63638.1};
GN OrderedLocusNames=Cla_0275 {ECO:0000313|EMBL:ACM63638.1};
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM63638.1, ECO:0000313|Proteomes:UP000007727};
RN [1] {ECO:0000313|EMBL:ACM63638.1, ECO:0000313|Proteomes:UP000007727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060
RC {ECO:0000313|Proteomes:UP000007727};
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|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.
CC {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR EMBL; CP000932; ACM63638.1; -; Genomic_DNA.
DR RefSeq; WP_012661022.1; NC_012039.1.
DR AlphaFoldDB; B9KF03; -.
DR STRING; 306263.Cla_0275; -.
DR GeneID; 7410184; -.
DR KEGG; cla:CLA_0275; -.
DR PATRIC; fig|306263.5.peg.273; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_7; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000007727; 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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:ACM63638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007727}.
FT DOMAIN 11..305
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 368..436
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 466 AA; 52701 MW; 77B9F79AE381A7AC CRC64;
MSQKAEKLWG GRFDLPTNKL VEEYTASLLV EPRLAPFDIQ GSIVHAKMLA KEGIIKEDEA
KTIIKGLEQV KEEIQNGSFV FDIADEDIHM AIEKRMTQIV GSVGGKLHTA RSRNDQTTLD
SKMHMRAVIK EILNQIIALQ EEIINQAQKN IKAIMPGYTH LQTGQPVLFS HWIMAYFWML
SRDYSRFEDL YKRMNECPLG AAALGGTTFN IDRHFCAKEL GFAKPTENSI DSVSDRDHMV
EFTSVAAMCF MHLSRFCEEL ILFSSQDFKF IELSDDFCTG SSIMPQKKNP DVAEKMRGKT
GRMYGNVMAM LTIMKGIPLA YNTDMSEDKA QVYDSMDTLM ASLKIITPMI EKMQVNADNT
KAAAAKGFSN ATDMADYLVR KNIPFRKAHE IVGLAVNYCI KNGKMLEELS LKEFHQFNEN
IQDDIYEAIA LQTCVDARLS YGGTGTKVVL EQIKHAKEFL EKLKKD
//
