Q97GL0 (SYFB_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase beta subunit
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name=PheRS

Gene names

Name:	pheT
Ordered Locus Names:	CA_C2356

Organism

Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]

Taxonomic identifier

272562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium acetobutylicum

Protein attributes

Sequence length	792 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00283
Cofactor	Binds 2 magnesium ions per tetramer By similarity.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. Contains 1 B5 domain. Contains 1 FDX-ACB domain. Contains 1 tRNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP phenylalanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 792	792	Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283		PRO_0000126870
Regions
	Domain	39 – 150	112	tRNA-binding
	Domain	404 – 479	76	B5
	Domain	699 – 792	94	FDX-ACB
Sites
	Metal binding	457	1	Magnesium By similarity
	Metal binding	463	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	466	1	Magnesium By similarity
	Metal binding	467	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97GL0 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 9BD754AA12E6707D	FASTA	792	88,781
	10 20 30 40 50 60 MKVPVKWLKD YVDFDINAKE LGDRLTLSGS KVEEIITSGD EITNVVTGKI LKIDPHPDAE 70 80 90 100 110 120 KLVICSVDVG KNEPIQIVTG AQNMKENDIV PVALHGSTLP GGVKIKKGKL RGVVSNGMMC 130 140 150 160 170 180 AKEELGIADE EHVHGLMILD ENTPIGKDIK EVLGLDNPVI DFEITSNRPD CLSVIGIARE 190 200 210 220 230 240 TAATINTKYR NVKIDFSETK GRNIKEELEV EVKDKLCRRY MARVIKNVKI EDSPAWMQER 250 260 270 280 290 300 LMLAGVRPIN NIVDITNFVM LEVGQPMHAF DKKMITSNKI VIERAKDGEK FTTLDSEERS 310 320 330 340 350 360 LDSNVLMIKD GDKNCAIAGI MGGLDSEVAE NTHEIIFESA NFDGTNIRVS SQKLALRTEA 370 380 390 400 410 420 SGRYEKDLDP NLAEIALNRA CTLIQELNAG EIVEGVIDIY PVKSEPNIVE VDYNWINNFL 430 440 450 460 470 480 GIKISKEEMK EYLDRLELTT EIKGDKLEVF SPTFRCDINI KEDVAEEVAR IYGYNKVPST 490 500 510 520 530 540 TVKSQSIRTG KSKIQQIKDV VTDILISSGL NESINYSFVS PKIFDKILVP EDSELRNVVK 550 560 570 580 590 600 IRNPLGEDFS VMRTTTLHSM MESLARNYSH NNELAKLFEI GKVYIPSENE GEIPKERNVI 610 620 630 640 650 660 TIGMYGNVDY FDLKGVVENL VEILGVNKIS YARESENPTF HPGKTAVIKI KNTVLGTLGE 670 680 690 700 710 720 VHPDVCENYE VEERCYVAEI DLDLLLENVS LSRKYKALPK FPTVTRDISV LVDEDILVQE 730 740 750 760 770 780 IENVIKRQGG TILESLNLFD VYKGKQVPQG KKSVSYALTY RDENKTLTDK DVEKIQNKVI 790 KTLEHVLGAE LR

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK80312.1.
PIR	E97190.
RefSeq	NP_348972.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97GL0.
ModBase	Search...
Protein-protein interaction databases
STRING	272562.CA_C2356.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK80312; AAK80312; CA_C2356.
GeneID	1118539.
KEGG	cac:CA_C2356.
PATRIC	32039079. VBICloAce74127_2552.
Phylogenomic databases
eggNOG	COG0072.
HOGENOM	HOG000292087.
KO	K01890.
OMA	MKFSEQW.
ProtClustDB	PRK00629.
Enzyme and pathway databases
BioCyc	CACE272562:GJIH-2405-MONOMER.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.30.56.20. 1 hit. 3.30.70.380. 1 hit. 3.50.40.10. 1 hit.
HAMAP	MF_00283. Phe_tRNA_synth_beta1.
InterPro	IPR005146. B3/B4_tRNA-bd. IPR009061. DNA-bd_dom_put. IPR012340. NA-bd_OB-fold. IPR004532. Phe-tRNA-ligase_IIc_bsu_bac. IPR020825. Phe-tRNA_synthase_B3/B4. IPR005121. PheS_beta_Fdx_antiC-bd. IPR002547. tRNA-bd_dom. IPR005147. tRNA_synthase_B5-dom. [Graphical view]
Pfam	PF03483. B3_4. 1 hit. PF03484. B5. 1 hit. PF03147. FDX-ACB. 1 hit. PF01588. tRNA_bind. 1 hit. [Graphical view]
SMART	SM00873. B3_4. 1 hit. SM00874. B5. 1 hit. SM00896. FDX-ACB. 1 hit. [Graphical view]
SUPFAM	SSF56037. B3_4. 1 hit. SSF54991. Fdx_AntiC_bd. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit. SSF46955. Putativ_DNA_bind. 1 hit.
TIGRFAMs	TIGR00472. pheT_bact. 1 hit.
PROSITE	PS51483. B5. 1 hit. PS51447. FDX_ACB. 1 hit. PS50886. TRBD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYFB_CLOAB

Accession

Primary (citable) accession number: Q97GL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program