ID A0A0S2JC64_9GAMM Unreviewed; 644 AA.
AC A0A0S2JC64;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CMT41_01970 {ECO:0000313|EMBL:ALO33618.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO33618.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO33618.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO33618.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) 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;
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 ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552,
CC ECO:0000256|PIRNR:PIRNR036456}.
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DR EMBL; CP013145; ALO33618.1; -; Genomic_DNA.
DR RefSeq; WP_057179490.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JC64; -.
DR STRING; 58049.CMT41_01970; -.
DR KEGG; com:CMT41_01970; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000065319; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR011244; ASAL_AGS_AcTrfase.
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; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PIRSF; PIRSF036456; ASAL_AGS; 2.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036456}.
FT DOMAIN 492..642
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 644 AA; 71307 MW; 9A985A38BCB24773 CRC64;
MALWGGRFKG KASLQFKKFN DSLPIDYRMA VQDIVGSIAW AQAIHEVGVL NDDELVRLTA
ALEELKASVE ENPQQILLSD AEDIHSWVEI QLIEKIGDLG KKLHTGRSRN DQVATDLKLW
CKETGGDLLF ALVNLQQAMM NLAEREKDTV LPGYTHLQRA QPITFGHWCL AYVEMFDRDI
GRLKDALYRL DVSPLGSGAL AGTAYPIDRK ALAHRLGFRT ATLNSLDAVS DRDHVIELLA
SASISMMHLS RFAEDLIFYN SGEAGFVEMS DLVSSGSSLM PQKKNPDACE LIRGKTGRVF
GALTGMLTTM KALALAYNKD MQEDKEGLFD ALDTWQECME MAVLVADGLK VNRSRTLAAA
QQGYANATEL ADYLVGKDIP FREAHHIVGE VVLAAIDKAV PLEDLTITQL QAFSDKIEQD
VYQHLTIEST LNKREVLGGT SRAQVEKALA TTQSGNEAIL NEQVVGAPGK QQIQVALKQV
KQRLNAQRAA AMSVRRAKMS DVDSIHQLVN FWADKGEILP RSRDNIIHDI QNFVVTELEG
KVVGTASLYI YQTGLAEIRS VVVDESAQQQ GQGEALVQYL LEFAHQMELA QIIVLTYIPQ
YFEQLGFNLI DKNSLAENII EDSEPSPHKD PADEVAMAYI LNQP
//
