P33074 (SDHB_PEPAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-serine dehydratase, beta chain
Short name=SDH
EC=4.3.1.17

Alternative name(s):
L-serine deaminase
Short name=L-SD

Gene names

Name:

sdhB

Organism

Peptostreptococcus asaccharolyticus (Peptococcus asaccharolyticus)

Taxonomic identifier

1258 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XI. Incertae Sedis › Peptoniphilus

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-serine = pyruvate + NH3.
Cofactor	Binds 1 4Fe-4S cluster.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Heterooctamer of four alpha chains and four beta chains.
Sequence similarities	Belongs to the iron-sulfur dependent L-serine dehydratase family. Contains 1 ACT domain.

Ontologies

Keywords
Biological process	Gluconeogenesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW L-serine ammonia-lyase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 222	222	L-serine dehydratase, beta chain		PRO_0000171918
Regions
	Domain	149 – 220	72	ACT

Sequences

	Sequence		Length	Mass (Da)
	P33074 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 3A2A624EC3104C08	FASTA	222	24,151
	10 20 30 40 50 60 MTDYSAFEVM GPIMVGPSSS HTAGACKIAN VATSIVSNNY NQVEFQLHGS FAHTFKGHGT 70 80 90 100 110 120 DRALVGGILG FEPDDDRIKT SFELAKQAGL NYIFTTTNLG DNYHPNSVKI VFSYPNGEEE 130 140 150 160 170 180 YVIGSSIGGG AMKIVNINGI AIEFRGEYST ILLEYPEQRG VISYVSSLLT GSEYNIESLN 190 200 210 220 TKKNKLTNIV TLTVEIDKPL TESLKSAILG VERFTTAKYV EV

References

[1]

"Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli." Hofmeister A.E., Textor S., Buckel W. J. Bacteriol. 179:4937-4941(1997) [PubMed: 9244285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14963 / DSM 20463 / NCIB 10074 / NCTC 11461.

[2]

"Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus." Grabowski R., Buckel W. Eur. J. Biochem. 199:89-94(1991) [PubMed: 2065681] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-19. Strain: ATCC 14963 / DSM 20463 / NCIB 10074 / NCTC 11461.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U76260 Genomic DNA. Translation: AAC45545.1.
PIR	S16376.
3D structure databases
ProteinModelPortal	P33074.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR004643. Fe-S_L-Ser_bsu. IPR005131. Ser_deHydtase_bsu. [Graphical view]
Pfam	PF03315. SDH_beta. 1 hit. [Graphical view]
PIRSF	PIRSF036692. SDH_B. 1 hit.
TIGRFAMs	TIGR00719. Sda_beta. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SDHB_PEPAS

Accession

Primary (citable) accession number: P33074

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	July 15, 1999
Last modified:	May 31, 2011
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program