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Database: UniProt/SWISS-PROT
Entry: ARLY_METST
LinkDB: ARLY_METST
Original site: ARLY_METST 
ID   ARLY_METST              Reviewed;         465 AA.
AC   Q2NGN7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   29-OCT-2014, entry version 64.
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};
GN   OrderedLocusNames=Msp_0618;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine. {ECO:0000255|HAMAP-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:0000255|HAMAP-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; CP000102; ABC57016.1; -; Genomic_DNA.
DR   RefSeq; WP_011406216.1; NC_007681.1.
DR   RefSeq; YP_447659.1; NC_007681.1.
DR   ProteinModelPortal; Q2NGN7; -.
DR   STRING; 339860.Msp_0618; -.
DR   EnsemblBacteria; ABC57016; ABC57016; Msp_0618.
DR   GeneID; 3855335; -.
DR   KEGG; mst:Msp_0618; -.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KEGIFDA; -.
DR   BioCyc; MSTA339860:GJEZ-618-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
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; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN         1    465       Argininosuccinate lyase.
FT                                /FTId=PRO_0000240791.
SQ   SEQUENCE   465 AA;  52209 MW;  A48E83EBDCB8B668 CRC64;
     MDLRAGRFDG QMTDDAAQFS SSIEFDKRIF KSDIKCNRAH TTMLIEEGII PKESGKKILK
     ALDKLEKEGI GALNLDPSFE DIHMALEDYV TKEIGDEAGF MHTAKSRNDQ VCTDIRLTLK
     EEIENTISNI KSFIKTIVEM AKENTHTLFI AYTHLQHAQP TTFAHHLMAY ANELRRDCER
     LIDTYKRVDM NPLGSAALTT TGFPINRERT TELLGFSKVM DNSIDGVSSR DFAAEAIFDY
     AMLSTTLGKI SDEIVIWSSY EFRMVECSNQ YSSTSSIMPQ KKNPDIAELS RGKSTIAYGE
     LMTVLSMIKG IPHSYNRDLQ EVTPHLWNAI DNTNDILRIV HGMLSTLTIN KDRTEELAGA
     NFATATELAD VMVREKNLPF RTAHRIVGRV VSEAIDDNIT THDIDNDYVN RVSVEVMGKP
     INLGEDLVKQ ALNPLRNVKS RTVIGGCAPE AVNDAIEKME IFLNE
//
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