Reviewed, UniProtKB/Swiss-Prot Q608S3 (HIS82_METCA)

Names and origin

Protein names

Recommended name:
    Histidinol-phosphate aminotransferase 2
    EC=2.6.1.9
Alternative name(s):
    Imidazole acetol-phosphate transaminase 2

Gene names

Name:	hisC2
Synonyms:	hisC-2
Ordered Locus Names:	MCA1417

Organism

Methylococcus capsulatus [Complete proteome] [HAMAP]

Taxonomic identifier

414 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 371	371	Histidinol-phosphate aminotransferase 2 HAMAP MF_01023		PRO_0000153392
Amino acid modifications
	Modified residue	232	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q608S3-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 6A4872377A5F1C91	FASTA	371	39,708
	10 20 30 40 50 60 MSITTLAVPG VRGLTPYQPG KPIGELEREF ALKRIVKLAS NENPLGASPK VLEVVRRILG 70 80 90 100 110 120 GTHLYPDGSG FELKAALAEK LGVEPAQIVL GNGSNDVLDL VARAFLTAGR NAVYSEYAFA 130 140 150 160 170 180 VYPIATQTAG ATGKTAPAHD GSRGPRFGHD LETMLERVDP DTRVVFIANP NNPTGTLLGR 190 200 210 220 230 240 GELYSFLAAL PEHVIAVVDE AYFEYARRPD HPDALEWLGE FPGLIVTRTF SKAYGLAGLR 250 260 270 280 290 300 VGYAVTGVEI ADLLNRARQP FNVNTLGLAA AAAALEDTGF LEATVQANDA GRSQLEAGFR 310 320 330 340 350 360 ERGFDFIPSA GNFVSFDLGR PATPVFDALL REGVIVRPLG NYGLPNHLRV SVGTAEEIDL 370 FFAALDRVLV P

References

[1]

"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017282 Genomic DNA. Translation: AAU92305.1.
RefSeq	YP_113874.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3102073.
GenomeReviews	Gene locus MCA1417 in contig AE017282_GR.
KEGG	mca:MCA1417.
NMPDR	fig|243233.4.peg.783.
TIGR	MCA1417.
Phylogenomic databases
HOGENOM	HBG646350.
OMA	KGYIVRS.
Enzyme and pathway databases
BioCyc	MCAP243233:MCA_1417-MONOMER.
BRENDA	2.6.1.9. 2172.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001176. ACC_synthase. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
TIGRFAMs	TIGR01141. hisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS82_METCA

Accession

Primary (citable) accession number: Q608S3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)