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Database: UniProt
Entry: U2Q0M0_9CLOT
LinkDB: U2Q0M0_9CLOT
Original site: U2Q0M0_9CLOT 
ID   U2Q0M0_9CLOT            Unreviewed;       461 AA.
AC   U2Q0M0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   13-SEP-2023, entry version 43.
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   ORFNames=CINTURNW_3112 {ECO:0000313|EMBL:ERK29554.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK29554.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK29554.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK29554.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT   Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(2013).
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}.
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:ERK29554.1}.
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DR   EMBL; APJA01000016; ERK29554.1; -; Genomic_DNA.
DR   RefSeq; WP_021803082.1; NZ_KI273145.1.
DR   AlphaFoldDB; U2Q0M0; -.
DR   STRING; 1294142.CINTURNW_3112; -.
DR   PATRIC; fig|1294142.3.peg.3240; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000016721; Unassembled WGS sequence.
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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016721}.
FT   DOMAIN          6..300
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          363..431
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   461 AA;  51864 MW;  19CAC37A940117A8 CRC64;
     MKLWGGRFQK AVDNLVNDFN SSIRTDGRMF KEDIDGSLAH VKMLIAQDII PKQDGEKIIS
     GLTEISKRIE NGVIEIDPSS EDIHSFIEAT LTYYIGDEGK KLHTGRSRND QVTLDTRLYL
     KKELKNLINV ILSFEETLLI KAEENIDTIM PGYTHMQKAQ PITFAHHLLA YGEMFKRDLG
     RIKDALKRMD EMPLGSGALA TSTYPIDREM VAKELDFASI SLNSLDAVSD RDYVIETLSA
     LSMIMMHLSR FSEEVILWCT HEFSFIELDD AYSTGSSIMP QKKNPDVAEL VRGKTGRVYG
     DLITLLTLMK GIPLAYNKDM QEDKEALFDA LDTVFLSIKT FNGMLKTMRI KKDNMRKGAL
     GGFTNATDVA DYLVKKGVAF RNAHEVVGAI VLHCINKGIN IEELSLEALK EFSSYFEEDI
     YNAISLETCV EERKVIGGPS SKSVKIQLEA LKNFIDNNKI V
//
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