B4SGW1 (GSA_PELPB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase
Short name=GSA
EC=5.4.3.8

Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT

Gene names

Name:	hemL
Ordered Locus Names:	Ppha_2800

Organism

Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]

Taxonomic identifier

324925 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon › Pelodictyon phaeoclathratiforme

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule MF_00375
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00375.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity 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 – 431	431	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_1000121906
Amino acid modifications
	Modified residue	269	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4SGW1 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 8FE98194DB7E7C7F	FASTA	431	46,146
	10 20 30 40 50 60 MPQLTKSAEL FEKAKKFIPG GVNSPVRAFK SVGGTPVYMA KGSGAYMTDV DGNTYLDYVG 70 80 90 100 110 120 SWGPFILGSM HPRITAALEY TLKNIGTSFG TPIEMEIEIA ELLCKIVPSL EMVRMVNSGT 130 140 150 160 170 180 EATMSAVRLA RGYTGRDKII KFEGCYHGHG DSFLIKAGSG ALTLGAPDSP GVTKGTAMDT 190 200 210 220 230 240 LNATYNDIDS VKLLVNENKG QIAAIIIEPV AGNTGVIPAK PGFLAALREL CTEEGIVLIF 250 260 270 280 290 300 DEVMCGFRVA LGGAQSLYGV TPDLTTMGKI IGGGLPVGAF GGKREIMERV APLGDVYQAG 310 320 330 340 350 360 TLSGNPLALT AGLETLKILI DENPYPELER KAVILESGFN DNLKKLGLNY VQNRVGSMSC 370 380 390 400 410 420 LFFTETPVVD YSTAVTADTK RHGKYFHSML DQGIYLAPSQ FEAMFISFMH TDEDLEKTIK 430 ANYNALVASG Q

References

[1]

"Complete sequence of Pelodictyon phaeoclathratiforme BU-1." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. , Overmann J., Bryant D.A., Richardson P. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001110 Genomic DNA. Translation: ACF44949.1.
RefSeq	YP_002019566.1. NC_011060.1.
3D structure databases
ProteinModelPortal	B4SGW1.
SMR	B4SGW1. Positions 1-423.
ModBase	Search...
Protein-protein interaction databases
STRING	324925.Ppha_2800.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACF44949; ACF44949; Ppha_2800.
GeneID	6461159.
KEGG	pph:Ppha_2800.
PATRIC	22906457. VBIPelPha134556_2984.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	FNGNPIS.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	PPHA324925:GHBF-2852-MONOMER.
UniPathway	UPA00251; UER00317. UPA00668.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_00375. HemL_aminotrans_3.
InterPro	IPR004639. 4pyrrol_synth_GluAld_NH2Trfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit. PTHR11986:SF5. PTHR11986:SF5. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00713. hemL. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA_PELPB

Accession

Primary (citable) accession number: B4SGW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program