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Database: UniProt
Entry: I7LK85_9CLOT
LinkDB: I7LK85_9CLOT
Original site: I7LK85_9CLOT 
ID   I7LK85_9CLOT            Unreviewed;       439 AA.
AC   I7LK85;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=CAAU_2184 {ECO:0000313|EMBL:CCJ34268.1};
OS   Caloramator australicus RC3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Caloramator.
OX   NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ34268.1, ECO:0000313|Proteomes:UP000007652};
RN   [1] {ECO:0000313|EMBL:CCJ34268.1, ECO:0000313|Proteomes:UP000007652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC3 {ECO:0000313|EMBL:CCJ34268.1,
RC   ECO:0000313|Proteomes:UP000007652};
RX   PubMed=21421756; DOI=10.1128/JB.00193-11;
RA   Ogg C.D., Patel B.K.C.;
RT   "Draft genome sequence of Caloramator australicus strain RC3T, a
RT   thermoanaerobe from the Great Artesian Basin of Australia.";
RL   J. Bacteriol. 193:2664-2665(2011).
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:CCJ34268.1}.
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DR   EMBL; CAKP01000113; CCJ34268.1; -; Genomic_DNA.
DR   RefSeq; WP_008909524.1; NZ_CAKP01000113.1.
DR   AlphaFoldDB; I7LK85; -.
DR   STRING; 857293.CAAU_2184; -.
DR   eggNOG; COG0165; Bacteria.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007652; 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:UP000007652}.
FT   DOMAIN          7..300
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          363..430
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   439 AA;  50498 MW;  5D7CFB282762B7CD CRC64;
     MKKLWGGRFE KVENPLMKKF NSSFEIDKRL IFDDIEGSIA HTKMLTKVGI LREEEGSKII
     NGLEEILEDI KSGKLELIGD FEDVHSFVEF HLIQRIGILG KKLHTARSRN DQVVTDLKLF
     LKRECSIIIE KIKFLQQTIK KKADENPYIM AGFTHLQPAQ VITFRHYLMA YFNMLERDKR
     RIQNAIDIMD ECPLGSCALA GTTYDIDREF TAKVLGFKKP VENFLDGVSD RDFVLEILSD
     LSIIMMHLSR ISEDFIIYSS CQFKFITLDD EFSTGSSIMP QKKNPDSLEL IRGKTGRVYG
     NLMALLTTLK GLPLAYNKDM QEDKEAIFDS LDTVKNCLDI LEGVIRTLKV NEEKILKAIE
     DGYLNATEVA DYLVNKGVPF RDAHRIVGKI VLFCEEKGKN INELSLEEFK GFSSLFEEDI
     YDFIDYYKIL NRGIKKIML
//
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