P31572 (CAIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Crotonobetainyl-CoA:carnitine CoA-transferase
EC=2.8.3.-

Gene names

Name:	caiB
Synonyms:	yaaN
Ordered Locus Names:	b0038, JW0037

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. HAMAP-Rule MF_01050
Pathway	Amine and polyamine metabolism; carnitine metabolism. HAMAP-Rule MF_01050
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_01050.
Induction	By L-carnitine or crotonobetaine. HAMAP-Rule MF_01050
Miscellaneous	Some strains of E.coli, such as ATCC 25922, can metabolize carnitine under aerobiosis. HAMAP-Rule MF_01050
Sequence similarities	Belongs to the CaiB/BaiF CoA-transferase family.
Caution	Was originally (Ref.1) thought to be an L-carnitine dehydratase.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carnitine catabolic process Inferred from experiment Ref.1. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	CoA-transferase activity Inferred from electronic annotation. Source: HAMAP carnitine dehydratase activity Inferred from experiment Ref.2Ref.1. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 405

405

Crotonobetainyl-CoA:carnitine CoA-transferase HAMAP-Rule MF_01050

PRO_0000194708

Sites

Active site

169

1

Nucleophile

Binding site

97

1

Coenzyme A

Binding site

104

1

Coenzyme A

Natural variations

Natural variant

187

1

V → A in strain: O44:K74.

Natural variant

302

1

T → A in strain: O44:K74.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

405

Helix Strand Turn

Details...

Turn

11 – 14

4

Beta strand

16 – 20

5

Helix

25 – 35

11

Beta strand

39 – 44

6

Beta strand

46 – 48

3

Helix

51 – 54

4

Beta strand

55 – 57

3

Helix

58 – 62

5

Turn

63 – 65

3

Beta strand

67 – 71

5

Beta strand

73 – 75

3

Helix

76 – 86

11

Beta strand

90 – 95

6

Beta strand

97 – 99

3

Helix

100 – 103

4

Helix

108 – 114

7

Beta strand

119 – 126

8

Beta strand

128 – 130

3

Turn

132 – 136

5

Helix

141 – 147

7

Helix

151 – 153

3

Beta strand

154 – 156

3

Turn

164 – 166

3

Helix

167 – 190

24

Beta strand

194 – 199

6

Helix

200 – 207

8

Helix

209 – 216

8

Beta strand

231 – 233

3

Beta strand

236 – 241

6

Beta strand

244 – 249

6

Helix

253 – 263

11

Helix

266 – 268

3

Beta strand

271 – 274

4

Turn

283 – 285

3

Helix

289 – 301

13

Helix

305 – 314

10

Beta strand

318 – 321

4

Helix

325 – 327

3

Helix

332 – 337

6

Beta strand

340 – 344

5

Beta strand

350 – 354

5

Beta strand

361 – 363

3

Turn

374 – 377

4

Helix

378 – 384

7

Helix

389 – 397

9

Beta strand

400 – 402

3

Sequences

	Sequence		Length	Mass (Da)
	P31572 [UniParc]. Last modified February 1, 1995. Version 3. Checksum: 75583684B4B5A2DE	FASTA	405	45,127
	10 20 30 40 50 60 MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ 70 80 90 100 110 120 LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI 130 140 150 160 170 180 AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA 190 200 210 220 230 240 LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK 250 260 270 280 290 300 CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL 310 320 330 340 350 360 ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF 370 380 390 400 KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase." Eichler K., Schunck W.-H., Kleber H.-P., Mandrand-Berthelot M.-A. J. Bacteriol. 176:2970-2975(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19. Strain: O44:K74.
[2]	"Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli." Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A. Mol. Microbiol. 13:775-786(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O44:K74.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli." Elssner T., Engemann C., Baumgart K., Kleber H.-P. Biochemistry 40:11140-11148(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: O44:K74.
[7]	"Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions." Elssner T., Preusser A., Wagner U., Kleber H.-P. FEMS Microbiol. Lett. 174:295-301(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY UNDER AEROBIOSIS. Strain: ATCC 25922 / DSM 1103 / NCIB 12210 and O44:K74.
[8]	"Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism." Stenmark P., Gurmu D., Nordlund P. Biochemistry 43:13996-14003(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67748 Genomic DNA. Translation: CAA47971.1.
X73904 Genomic DNA. Translation: CAA52112.1.
U00096 Genomic DNA. Translation: AAC73149.1.
AP009048 Genomic DNA. Translation: BAB96607.1.

PIR

S40559.

RefSeq

NP_414580.1. NC_000913.2.
YP_488344.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XA3	X-ray	1.85	A/B	2-405	[»]
1XA4	X-ray	1.90	A/B	2-405	[»]
1XK6	X-ray	1.85	A/B/C/D	1-405	[»]
1XK7	X-ray	1.60	A/B/C	1-405	[»]
1XVT	X-ray	2.30	A	1-405	[»]
1XVU	X-ray	2.40	A	1-405	[»]
1XVV	X-ray	2.40	A	1-405	[»]

ProteinModelPortal

P31572.

SMR

P31572. Positions 1-405.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31572. 11 interactions.

STRING

511145.b0038.

Proteomic databases

PRIDE

P31572.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73149; AAC73149; b0038.
BAB96607; BAB96607; BAB96607.

GeneID

12932590.
948997.

KEGG

ecj:Y75_p0038.
eco:b0038.

PATRIC

32115171. VBIEscCol129921_0037.

Organism-specific databases

EchoBASE

EB1520.

EcoGene

EG11559. caiB.

Phylogenomic databases

eggNOG

COG1804.

HOGENOM

HOG000219745.

KO

K08298.

OMA

VMPKFKN.

ProtClustDB

PRK03525.

Enzyme and pathway databases

BioCyc

EcoCyc:CARNDEHYDRA-MONOMER.
ECOL316407:JW0037-MONOMER.
MetaCyc:CARNDEHYDRA-MONOMER.

UniPathway

UPA00117.

Gene expression databases

Genevestigator

P31572.

Family and domain databases

Gene3D

3.40.50.10540. 2 hits.

HAMAP

MF_01050. CaiB.

InterPro

IPR003673. CoA-Trfase_fam_III.
IPR023452. CoA-Trfase_fam_III_CaiB.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]

PANTHER

PTHR11837. PTHR11837. 1 hit.

Pfam

PF02515. CoA_transf_3. 1 hit.
[Graphical view]

SUPFAM

SSF89796. CoA-Trfase_fam_III. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P31572.

Entry information

Entry name

CAIB_ECOLI

Accession

Primary (citable) accession number: P31572

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program