ID A0A1B1PZQ9_9CHLB Unreviewed; 891 AA.
AC A0A1B1PZQ9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036,
GN ECO:0000313|EMBL:ANT64084.1};
GN ORFNames=Ptc2401_00281 {ECO:0000313|EMBL:ANT64084.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT64084.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT64084.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT64084.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000256|HAMAP-Rule:MF_00036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000256|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00036}.
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DR EMBL; CP016432; ANT64084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1PZQ9; -.
DR STRING; 1868325.Ptc2401_00281; -.
DR KEGG; proc:Ptc2401_00281; -.
DR PATRIC; fig|1868325.3.peg.268; -.
DR InParanoid; A0A1B1PZQ9; -.
DR Proteomes; UP000092496; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00036};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Reference proteome {ECO:0000313|Proteomes:UP000092496};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Zinc {ECO:0000256|HAMAP-Rule:MF_00036}.
FT DOMAIN 5..720
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 891 AA; 99454 MW; 50EB8F061F83F428 CRC64;
MPTGMKSQAI RTTFLEFFEA KEHKIVRSAP VIPAEDPTLL FTNAGMNQFK DVFLDKGSRP
YSRAVDTQKC IRASGKHNDL EDVGRDTYHH TFFEMLGNWS FGDYYKKEAI SWAWELMTDV
WKLPRERLYA TVYHDDEESL QIWKEATDIP HDHIMKFGDK DNFWEMGETG PCGPCSEIHI
DLTPDMSGAS LVNAGDHRVI ELWNLVFIQY DRQLDGSLQP LPKKHVDTGM GFERITAVLQ
GKNSNYDTDI FKPLFDAITE MTGISYRASL DGEHDIAMRV IADHARTLAF AIADGAMPGN
EGRGYVLRRI LRRALRYARK LDCRKPMLYK LIGVISETMG DVFPELRKQC GTVQKIVRSE
EESFLATLDR GMEIYGDIMA AMKTAGTTVM SGEDTFRLYD TYGFPVDLTR LMAEEEGCTI
DEAGFDACMQ EQKSRAREDR RQKHQVTEAE VAWHWFEEGA SHSRFCGYDQ LEADARILAF
RPAAEELLLI LDTTPFYAES GGQVGDQGVI ENGEYRFHVT DTRKDGDMII HIVDSIVNPT
DNTCIDPADI ASGFSQQVHA SVDRERRFDT ERNHTATHLL HAALRKVLGE HVQQKGSMVT
PERLRFDFSH FEKVSEKELA EVEAMVNREI REAHNLEKKA DIPFEEAVDM GALAFFGDKY
ADRVRVVEVP GISIELCGGT HVDNIGRIGL FKITGESSVA SGIRRIEAMT GKAAEELLWN
EFQELQQVRQ LLKARSDEGV AVKVQELLEE KKSLAKEMQD MQLSVLLQQA LQQLETAEEI
NGCKVLAMTF SDIDAGELRN LGQYIQDRMD DGVALLASSA GGKVALVSCV GQKALATRSL
NAGALVKSAA RAVQGGGGGK PAFATAGGKN PEGIPQALDI FREEVTAAIA G
//
