(data stored in ACNUC7421 zone)

SWISSPROT: D1CE80_THET1

ID   D1CE80_THET1            Unreviewed;       448 AA.
AC   D1CE80;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {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   OrderedLocusNames=Tter_0314 {ECO:0000313|EMBL:ACZ41236.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41236.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41236.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000256|HAMAP-
CC         Rule:MF_00006};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {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; CP001825; ACZ41236.1; -; Genomic_DNA.
DR   RefSeq; WP_012874271.1; NC_013525.1.
DR   STRING; 525904.Tter_0314; -.
DR   EnsemblBacteria; ACZ41236; ACZ41236; Tter_0314.
DR   KEGG; ttr:Tter_0314; -.
DR   eggNOG; ENOG4105CH7; Bacteria.
DR   eggNOG; COG0165; LUCA.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; TTER525904:G1GGS-318-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000323; Chromosome 1.
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; 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; 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;
DR   PRODOM; D1CE80.
DR   SWISS-2DPAGE; D1CE80.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:ACZ41236.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN       24    301       Lyase_1. {ECO:0000259|Pfam:PF00206}.
SQ   SEQUENCE   448 AA;  50108 MW;  26FC53965967A726 CRC64;
     MSKLWDKGYK LDETIERFEI GHDLAFDNEL VEVDVYGSIA HAEMLNRIGI LTDDELQTLK
     QGLGRILDLY RQGQFFMTPA DEDIHTKIEN FLVREYGDVG KKIHTARSRN DQVLVDLRLY
     AKAKILELES ALLQCAESLV EFASKHEHVP MPGYTHMQRA MLSSVGTWAG AFAEALLDDL
     KLLETAYELN DQSPLGSAAS YGVPLPIDRQ YVADKLGFAK VQNNVLYAQN ARGKFEALVV
     QAISQIMLDL SKLAQDILLF TTAEYGFFTI SDSFVTGSSI MPQKKNLSMM ELIRAKANMA
     LGYQQQMMSV LSGLPSGYNK DYQETKKPFM EAIQLALDSL KVAELTISNL SPNKDKLLAA
     CTPELFATDK AYELVQQGMP FRDAYRYVGT NLDKLEGADP EESLKKRTHI GASGNLGLSK
     LKESISASKV NVDKKYSHLM ETWQNLLS
//

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