ID CRNS1_CHICK Reviewed; 930 AA.
AC D3KCC4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Carnosine synthase 1 {ECO:0000305|PubMed:20097752, ECO:0000312|EMBL:ADB91406.1};
DE EC=6.3.2.11 {ECO:0000269|PubMed:20097752};
DE AltName: Full=ATP-grasp domain-containing protein 1 {ECO:0000250|UniProtKB:A5YM72};
GN Name=CARNS1 {ECO:0000250|UniProtKB:A5YM72};
GN Synonyms=ATPGD1 {ECO:0000250|UniProtKB:A5YM72};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADB91406.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC TISSUE=Pectoralis muscle {ECO:0000312|EMBL:ADB91406.1};
RX PubMed=20097752; DOI=10.1074/jbc.m109.095505;
RA Drozak J., Veiga-da-Cunha M., Vertommen D., Stroobant V.,
RA Van Schaftingen E.;
RT "Molecular identification of carnosine synthase as ATP-grasp domain-
RT containing protein 1 (ATPGD1).";
RL J. Biol. Chem. 285:9346-9356(2010).
CC -!- FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine.
CC Carnosine is synthesized more efficiently than homocarnosine.
CC {ECO:0000269|PubMed:20097752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-alanine + L-histidine = ADP + carnosine + H(+) +
CC phosphate; Xref=Rhea:RHEA:19297, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57485,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:57966, ChEBI:CHEBI:456216;
CC EC=6.3.2.11; Evidence={ECO:0000269|PubMed:20097752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19298;
CC Evidence={ECO:0000305|PubMed:20097752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate + ATP + L-histidine = ADP + H(+) + L-
CC homocarnosine + phosphate; Xref=Rhea:RHEA:59568, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:59888, ChEBI:CHEBI:143075, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:20097752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59569;
CC Evidence={ECO:0000305|PubMed:20097752};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.033 mM for beta-alanine {ECO:0000269|PubMed:20097752};
CC KM=0.35 mM for 4-aminobutanoate {ECO:0000269|PubMed:20097752};
CC KM=0.10 mM for L-histidine {ECO:0000269|PubMed:20097752};
CC KM=1.42 mM for L-lysine {ECO:0000269|PubMed:20097752};
CC KM=1.62 mM for L-ornithine {ECO:0000269|PubMed:20097752};
CC KM=0.39 mM for N-methylhistidine {ECO:0000269|PubMed:20097752};
CC Vmax=119 nmol/min/mg enzyme toward beta-alanine
CC {ECO:0000269|PubMed:20097752};
CC Vmax=84.1 nmol/min/mg enzyme toward gamma-aminobutyrate
CC {ECO:0000269|PubMed:20097752};
CC Vmax=3.30 nmol/min/mg enzyme toward L-histidine
CC {ECO:0000269|PubMed:20097752};
CC Vmax=3.43 nmol/min/mg enzyme toward L-lysine
CC {ECO:0000269|PubMed:20097752};
CC Vmax=2.54 nmol/min/mg enzyme toward L-ornithine
CC {ECO:0000269|PubMed:20097752};
CC Vmax=3.51 nmol/min/mg enzyme toward N-methylhistidine
CC {ECO:0000269|PubMed:20097752};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20097752}.
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DR EMBL; GU453679; ADB91406.1; -; mRNA.
DR RefSeq; NP_001166064.1; NM_001172593.1.
DR AlphaFoldDB; D3KCC4; -.
DR SMR; D3KCC4; -.
DR STRING; 9031.ENSGALP00000055051; -.
DR GeneID; 100359387; -.
DR KEGG; gga:100359387; -.
DR CTD; 57571; -.
DR VEuPathDB; HostDB:geneid_100359387; -.
DR InParanoid; D3KCC4; -.
DR PhylomeDB; D3KCC4; -.
DR BRENDA; 6.3.2.11; 1306.
DR SABIO-RK; D3KCC4; -.
DR PRO; PR:D3KCC4; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0047730; F:carnosine synthase activity; IDA:UniProtKB.
DR GO; GO:0102102; F:homocarnosine synthase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035499; P:carnosine biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR041472; BL00235/CARNS1_N.
DR InterPro; IPR031046; CARNS1.
DR PANTHER; PTHR48066; CARNOSINE SYNTHASE 1; 1.
DR PANTHER; PTHR48066:SF1; CARNOSINE SYNTHASE 1; 1.
DR Pfam; PF18130; ATPgrasp_N; 1.
DR Pfam; PF15632; ATPgrasp_Ter; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..930
FT /note="Carnosine synthase 1"
FT /id="PRO_0000395311"
FT DOMAIN 624..825
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 650..716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 782
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 782
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 794
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 794
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 796
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 796
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 930 AA; 100060 MW; 5A152BDCD8E003F8 CRC64;
MISVDRLSEE QALGMKEQEW AGPEALCPGW QEEEVSDGEG PEDSGHPDPT AHAYEVLQHT
LRLEGMPLTI DRTGQPRTGS GPLDMTVCVL GSPTAFLPVL LEGGTRYPGA MVLCLAPAWA
SRVPSETSPG SWSLLLSRGV SFEAGGCTAL EEFVPPRRAT YVTGTFGSEG SWEGELARDL
DCPTGGSALL TRWLEDPLLS RWLLSARAGL PVPPTLAFIT GLWETLPEEP EPPGVHLVRL
QDPQGQESLV RDEVGAFLEG SSMQPYDQVA VRLSGWRWRG TDPHSTHRKV EGEAVAQAVA
ALLKGLREEE SILLEALVPT ARLPTLPPRS AAPRLPMALR ICTVVCRSWG DRPQLCQVAC
TAGRAEVPVR HGSALPLGLD SSLRQWGLAD AAQRQALAGQ LREAAEAAMA ALLAAEGELS
PAQRGGARAH TDVLGVDFLL ACVDGTLELV ALSANCLRCL ETCLLAEGMG HDVGQPAGDV
PRLLAECLLH RAQCHLVEGK DILLIGAGGV SKSFVWEAAR EYGLRIHLVE SDPEHFAAGL
VETFLPYDSR EHRRDEEHAE RVLEMLRARG LRPDACLSYW DDCVVLTALL CQRLGLPGCP
PAAVRLAKQK SRTHQHLQRC RRGRPPPAAF SVPCRRLRSH GDVERAAGAV PFPAVAKLEF
GAGAVGVRLV ENAGQCHAHA AQLWHDLRAD ADHPGIGLGW GNAMLLMEYV PGTEHDVDLV
LFEGRLLGAW VSDNGPTRVP TFLETAATLP SCLPADRQAQ LVRAALRCCR ACGLRHGVFN
VELKLSPAGP RLLEINPRMG GFYLRDWMRA VYGPDLLLAA VLLALGLPPV LPSRPAPRQQ
LAGVMCLASE HGRALRGGVM AALQGLQRRG LVRLNPLFEE AGGRYEEPCL SVACAGDGPA
EACGRLLGLC QALGIDSPQY PVGHFLSHFK
//
