ARLY_CHLPD
ID ARLY_CHLPD Reviewed; 464 AA.
AC A1BG31;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 82.
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=Cpha266_1327;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|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. {ECO:0000255|HAMAP-
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABL65358.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000492; ABL65358.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041467236.1; NC_008639.1.
DR AlphaFoldDB; A1BG31; -.
DR SMR; A1BG31; -.
DR STRING; 290317.Cpha266_1327; -.
DR PRIDE; A1BG31; -.
DR EnsemblBacteria; ABL65358; ABL65358; Cpha266_1327.
DR KEGG; cph:Cpha266_1327; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_10; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000008701; 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; 1.10.275.10; -; 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; 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; PF14698; ASL_C2; 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;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..464
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000321435"
SQ SEQUENCE 464 AA; 52511 MW; 3039AA6DACAF0505 CRC64;
MSDKKELLWQ SRFSEPFDRD ALRFSSSVHI DKALFREDIE GSIAHVTMLA EQDIISDAEC
ADLVQGLREI EEELASGTLV PHWEDEDIHT VIENRLKEKI GQTAGKIHSG RSRNDQVATD
TRLYLRKKIA ELQDAVQAMQ QMLIGKAETY KETIIFGYTH LQRAQPISAG HYYLAWFSMF
RRDRERLRDL LRRVNISPLG AAAFAGSTLP LNPARTAELL AFDDIFSNSI DAVSDRDILI
EFISACSIMM MHLSRFAEDL ILWSSYEFGY LEISDAFATG SSLMPQKKNA DIAELVRGKT
GRVYGNLVSM LTIMKGLPLS YNRDMQEDKQ PLFDTAETTI SSMRIFTKLI GHTTLKVERL
RSLTSEDLSL ATEIAEYLVS RNLPFREAHR ITGKIVTFSI GEGITLPRIT LEQFRTFSPL
FDSAIYDSLK PEASVNSKKS HGSCSFRSVE AQLAEARAQM QENR