Q8RJN5 (Q8RJN5_STEMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Peptide amidase EMBL CAC93616.1

Gene names

Name:

pam EMBL CAC93616.1

Organism

Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia) EMBL CAC93616.1

Taxonomic identifier

40324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Signal EMBL CAC93616.1
Technical term	3D-structure PDB 1M21 PDB 1M22
Gene Ontology (GO)
Molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Potential EMBL CAC93616.1
	Chain	38 – 540	503	peptide amidase EMBL CAC93616.1		PRO_5000067990
Sites
	Active site	202	1	Proton donor/acceptor PDB 1M21
	Active site	226	1	Nucleophile PDB 1M21
	Site	123	1	Important for catalytic activity PDB 1M21

Sequences

	Sequence		Length	Mass (Da)
	Q8RJN5 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: ABBA31F903C3EA02	FASTA	540	57,080
	10 20 30 40 50 60 MRPSLPPLLT CLLAALPALL SAGCSPATPS AHAAEPASRN VPFPYAETDV ADLQARMTAG 70 80 90 100 110 120 ELDSTTLTQA YLQRIAALDR TGPRLRAVIE LNPDALKEAA ERDRERRDGR LRGPLHGIPL 130 140 150 160 170 180 LLKDNINAAP MATSAGSLAL QGFRPDDAYL VRRLRDAGAV VLGKTNLSEW ANFRGNDSIS 190 200 210 220 230 240 GWSARGGQTR NPYRISHSPC GSSSGSAVAV AANLASVAIG TETDGSIVCP AAINGVVGLK 250 260 270 280 290 300 PTVGLVSRDG IIPISFSQDT AGPMARSVAD AAAVLTAIAG RDDADPATAT MPGRAVYDYT 310 320 330 340 350 360 ARLDPQGLRG KRIGLLQTPL LKYRGMPPLI EQAATELRRA GAVVVPVELP NQGAWAEAER 370 380 390 400 410 420 TLLLYEFKAG LERYFNTHRA PLRSLADLIA FNQAHSKQEL GLFGQELLVE ADATAGLADP 430 440 450 460 470 480 AYIRARSDAR RLAGPEGIDA ALAAHQLDAL VAPTTGVAWP IRSEGDDFPG ESYSAAAVAG 490 500 510 520 530 540 YPSLTVPMGQ IDGLPVGLLF MGTAWSEPKL IEMAYAYEQR TRARRPPHFD TDALIDAGEP

References

[1]	"Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia." Neumann S., Kula M.-R. Appl. Microbiol. Biotechnol. 58:772-780(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM 9181 EMBL CAC93616.1.
[2]	"An alternative mechanism for amidase signature enzymes." Labahn J., Neumann S., Buldt G., Kula M.R., Granzin J. J. Mol. Biol. 322:1053-1064(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 38-540, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ414049 Genomic DNA. Translation: CAC93616.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M21	X-ray	1.80	A/B	38-540	[»]
1M22	X-ray	1.40	A/B	38-540	[»]

ProteinModelPortal

Q8RJN5.

SMR

Q8RJN5. Positions 43-529.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.90.1300.10. 1 hit.

InterPro

IPR000120. Amidase.
IPR023631. Amidase_dom.
[Graphical view]

PANTHER

PTHR11895. PTHR11895. 1 hit.

Pfam

PF01425. Amidase. 1 hit.
[Graphical view]

SUPFAM

SSF75304. Amidase_sig_enz. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8RJN5.

Entry information

Entry name

Q8RJN5_STEMA

Accession

Primary (citable) accession number: Q8RJN5

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2002
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)